Manufacturing and Purification Processes of Complex Protein found in Fraction IV to make a separated Apo, Transferrin, and Alpha 1 Anti strepsin (A1AT) or A combined Transferrin/Apo/Human Albumin/A1AT and all new found proteins

ABSTRACT

A method of introducing healthy good human cells to eat up bad damaged cells, comprising administering an effective amount of a healthy good protein containing transferrin, alpha 1-antitrypsin, apolipoprotein A and human albumin. The method further comprises administering an effective amount of a protein containing ApoA1/2/4, or administering an effective amount of a protein containing Factor II, Factor VII, Factor IX and Factor X in prothrombin complex concentrate. The method can further comprise administering an effective amount of fibrinogen, Factor VIII, high concentrate fibrinogen, thrombin. hepatitis B immune globulin (HBIG), anti-thrombin III (AT-III), protein C, fibronectin, protein S and protein M.

CROSS REFERENCE TO RELATED APPLICATIONS

The present application is a division of prior application Ser. No.13/114,951, filed on May 24, 2011, which is hereby incorporated hereinby reference in its entirety and which is a continuation-in-part ofprior application Ser. No. 13/108,970, filed May 16, 2011, which ishereby incorporated herein by reference in its entirety and which is acontinuation-in-part of prior application Ser. No. 13/064,070, filedMar. 4, 2011, which is hereby incorporated herein by reference in itsentirety and which is a continuation-in-part of prior application Ser.No. 11/990,203, filed Jul. 15, 2008, which is hereby incorporated hereinby reference in its entirety. application Ser. No. 13/114,951 is acontinuation-in-part of prior application Ser. No. 12/457,796, filedJun. 22, 2009, which is hereby incorporated herein by reference in itsentirety and which is a continuation-in-part of prior application No.PCT/US 2007/020258, filed Sep. 19, 2007. The benefit under 35 USC 120 ishereby claimed of the filing dates of provisional application No.61/457,380, filed on Mar. 14, 2011 and provisional application No.61/457,380, filed on Mar. 14, 2011 and provisional application No.61/452,860, filed on Mar. 15, 2011 and provisional application No.61/472,930, filed on Apr. 7, 2011, all of which are hereby incorporatedherein by reference in their entireties.

A Complex of all proteins found currently in Plasma, Cryoprecipitate,Fraction III and newly found many proteins being indentified,Prothrombin Complex Concentrate (ProthoRAAS®), (Albumin (AlbuRAAS®)Factor VIII (HemoRAAS®), Fibrinogen (FibroRAAS®) High concentrateFibrinogen (FibrinGluRAAS®) Thrombin (ThrombiRAAS®) Thrombin for Fibrinsealant (FibrinGluRAAS), AT-III Protein, Protein C, Protein S, ProteinM, Protein G, Alpha 1 Anti Strepsin (A1AT), HDL ApoA1, ApoA2, ApoA4,Semenogelin-1, Haptoglobin, Vimentin, Nesprin-2 Interferon Alpha1/13, HPProtein, Vitamin B Binding, Alpha-Fetoprotein, Cask Protein, Alymloidprecursor, Neurexins, Syndecans, Protein rankl, and from otherantibodies Immuno globulins (GammaRAAS®), Hepatitis B Immune Globulin(Hepa RAAS®) Hepatitis A Antibodies, Cytomegalovirus Antibody, Anti-DAntibody, Zarizella Zoster Antibody, R SV Antibodies, SARS Antibody,H1N1 Antibodies, H1N5 Antibodies, West Nile Virus Antibody, or allantibodies in human or monoclonals, white blood cells, red blood cells,platelets, clyclomicron, electrolyses, albumin, globulins, peptides,tissues, placenta, catalase, All Factors, Cryoprecipitate, 5 FractionsI, II, III, IV, V of Human Blood and Plasma, Monoclonal antibodies,Recombinant DNA proteins, Transgenic proteins, particles, or anysubstances which are known proteins or unknown proteins which containGOOD HEALTHY CELLS and the combination of any of these Known or unknownproteins which contain any one of these GOOD HEALTHY cells Neutrophil,Lymphocyte, Eosinophil, Basophil, and MARCOPHAGE and Their potentialapplications for:

Schizophrenia, Cholesterol, Depression, AIDS, All Enveloped viruses (AllHepatitis A, B,C,D,E,G, SARS, H1N5, H1N1 and Non Envelope viruses, Cleanplaque, fat on liver, heart attack, stroke, Life span, Control ofObesity, control of Blood Pressure, Hypertension, Paralysis due to thestroke. All solid Tumor Cancers: AIDS related cancers, anal cancer,appendix cancer, bile duct, bladder, osteosarcoma, brain, breast,cervical, colon, esophagus, eye, gall bladder, gastric, othergastrointestinal, Intestines, head neck, heart, liver, hypopharyngeal,kidney, laryngeal, lip oral cavity, lung, mouth, nasal Parasal, ovarian,pancreas, parathyroid, penile, prostate, rectal, renal cell carcinoma,salivary, skin, Spleen, throat, testicular, urethral, Vaginal.Leukemia's, (Acute myeloid leukemia (M0-M7), lymphoma, marrowmalignancy, acute lymphoid leukemia (Small, middle, large) MDS, Myeloiddysfunction syndrome and Anemia.

SEPSIS, Hyper Inflammatory diseases, Acute Pancreatitis, AcuteRespiratory distress Syndrome, Ischemia reperfusion injury, Hepaticcirrhosis, RENAL FAILURE and Anti-oxidant. Alzheimer disease, AUSTISM,Parkinson, DIABETICS. Chemotherapy, radiotherapy and cytokine therapytoxicity, TNF and Stop Activation of HISTONE and ENDOTOXIN. Autoimmunediseases. Rheumatoid ARTHRITIS, Tuberculosis, Malarias. Lupus Sclerosisin brain, A1AT Deficiency, Emphysemea, LUNG CANCER, ASTHMA, Prion (Madcow), Anthrax and all Bacteria, Food Poisoning, Factor VII deficiencyand Surgery Hemophila A, Hemophila B, Wwb eventually will increasecoagulation, All other unknown viruses, bacteria infections, Healthycells replacement to maintain Youth fullness. Alpha 1 Anti Strepsin(A1AT), C1 Esterate Inhibitor and All inhibitors/Deficiencies in Humanbody.

Description of Invention and its Purposes:

Mankind have been suffering for hundreds of years for all kind ofdiseases, cancers, Alzheimer, diabetic, Parkinson, Autism and speciallythe agonies that we have to go through with AIDS, HEPATITIS B, andHEPATITIS C and new kinds of Virus infections and epidemic Incidencewhich feared and affected the economy of the world like SARS in China,Taiwan, Hong Kong, Vietnam, Singapore, Canada in 2003, with outbreak ofbird flu (H1 N5) 2004 in Europe, Vietnam, Thailand and most recently in2010 in Mexico with the outbreak of (H1 N1) which caused the country toshut down for weeks and badly affected its economy.

On the other hand, Most of countries in the World not only face withproblematic economies but also with The increased Healthcare cost foreach country. Such a health care system spends a lot of money forHealthcare which drags down economy.

Such an invention of these products will help save a lot of money forany country in Healthcare.

However the patients that benefit from these discoveries must understandtheir social responsibilities as they will live longer with very healthyconditions without Alzheimer, any kind of diseases, cancers, heartattack, stroke, and their prevention.

The definition of death is when the heart stops beating. AFODRAAS 1-85,AFCC 1-85 and ProthoRAAS® will clean up all plaque in our bodies to helpthe blood flow through all part of our bodies including the heart.AFODRAAS 1-85 (also referred to herein as “AFODRAAS 1”, “AFODRAAS” and“AFOD”) contains various combinations of apolipoproteins ApoA1, ApoA2,ApoA4, Apo-B48, ApoB100, ApoCI, ApoCII, ApoCIII, Apo-D, Apo-E, Apo-H,and Apo(a), all of which contain Good Healthy cells, as well as Alpha 1Antitrypsin (A1AT), which is known also to contain Good Healthy Cells,Transferrin, which contains Good Healthy Cells, and Human Albumin,another Good Healthy cell Protein, together with a group of at least 20unidentified discovered proteins which are being identified andcharacterized with the assistance of Academy of Science of China, thegroup containing Good Healthy cells. Each combination will be applied toa certain number of diseases, including solid and Blood cancers.

AFCC 1-85 (also referred to herein as “AFCCRAAS 1-85”, “AFCCRAAS 1”,“AFCCRAAS” and “AFCC”) contains various combinations of ProthrombinComplex Concentrate including all 13 Factors found in Fraction III,Alpha 1 Antitrypsin (A1AT), Transferrin, Human Albumin, and Antithrombin III, all of which contain Good healthy cell proteins. Thecombinations of AFCC 1-85 can also contain Transferrin, which containsGood Healthy Cells, and Human Albumin, another Good Healthy cellProtein, together with a group of at least 20 unidentified discoveredproteins which are being identified and characterized with theassistance of Academy of Science of China, the group containing GoodHealthy cells. Each combination will be applied to a certain number ofdiseases, including solid and Blood cancers.

The definition of death belongs to the beating of the heart, but if theLIVER will not manufacture, moderate, regulate and distribute Good Bloodcells to the heart, the heart will not function.

So in this discovery of invention: The LIVER has become the mostimportant ORGAN of the body as the liver Produce Antibodies and Proteinswhich are used to cure diseases and viruses as well as bacteriainfection. The liver is the largest organ in the body weightingapproximately 1.4 kg. It is located on the right side of belly. Rightunder the chest bone. It has two pieces. The right piece is larger andconsists of 3 smaller pieces together. The left piece is smaller, righton top of stomach adjacent to the throat. The structure of the liverconsists of from 50,000 to 100,000 small pieces with portal Vein in themiddle. From the portal vein, hundreds of liver cells mix with pilesystem and very tiny blood vessels. With approximately 300 billion ofcells (Approximately 30% of a trillion of cells in our body. It has theAbility to restore and maintain its function in case for any reason ithas lost 90% of the liver. None of other Organ which has only 10% canfunction in our body. If 100% of the liver has been damaged due to thediseases a person can only live with a piece of Liver transplant. Theliver receives blood through portal vein and Arterial vein. Every minuteall these blood vessel has transferred to liver approximately 1.5 literof blood. Blood in Arterial vein contain plenty of oxygen as for Bloodin portal vein transport all waste from digestion. Liver is consideredas a sophisticated chemical manufacturer/moderator/regulator/distributorwith hundreds of Different important tasks:

1. Liver is the warehouse to receive glucose from small intestine storeas Glycogen. After each meal, when the blood pressure increases, insulinfrom pancreas will help the liver to transform Glucose into glycogen. Ina few hours later when the blood pressure decreases, the liver again totransform Glycogen into glucose then send Glucose to the blood thendistribute to other organs or components which need Glucose. Diabeticpeople cannot receive insulin produced by pancreas due to theaccumulation of Glucose from foods in the liver.2. Beside the above task, liver also transform glucose and fat intoprotein and it also transform protein and fat into glucose.3. The liver produces approximately 0.5-0.9 liter of pile every day.Pile is a liquid with the YELLOW-BLUE color,

It is bitter with its most important structure is Pile SALT which isnecessary for the digestion of Fat in the foods.

4. Liver can eliminate some toxicity like alcohol and a few drugs likeacetaminophen.5. The liver produces urea, a waste from the protein and eliminatethrough kidney.6. THE LIVER DESTROY ALL DAMAGED OR OLD RED CELLS as well DESTROY ALLBACTERIA in the Foods in the intestine.7. The Liver contains Vitamins, A, B, D, E and K8. Liver creates the protein in the blood like Albumin, Globulin andCoagulation.

FAT on the Liver:

When learning about the Fat on the Liver, people usually feel surprisedand scared and question how could One survives with FAT on the liver. Inreality, Liver like other organs of our body, everywhere we have FAT.

FAT is a creative element of CELLS. Whenever FAT in the liver exceedsaround 5% of the liver, attack and occupy All healthy cells then therewill be a problem. At this time, Liver will have a Fatty Yellow color,the liver becomes bigger and heavier than its normalcy.

Cut a piece of the liver without disease, through microscope, we see theblood full of in space between the liver cells.

Tissue factor cells surrounding blood vessels will take away TOXICITY,BACTERIA, FAT to Transform Blood into CLEANER. Liver is like a filter.If now in liver cells and the space between the liver cells, are full ofFAT

Then the FILTRATION and OTHER FUNCTIONS of the Liver will decrease andlead one to bad consequence.

All FAT majorities of them belong to TRYGLYCERIDES.

In our pre animal clinical study using Lab scale product of AFODRAAS(1-85) A total of 14 rabbits out of 60 Died during the 10 weeks of HighFAT DIET Feed due to stomach and fat accumulation on the liver.

MACROPHAGE (in Greek language BIG EATERS from makros “Large”+Phagein(EAT) are WHITE BLOOD CELLS produced by the differentiation of Monocytesin tissues. Human macrophages are about 21 micrometers in diameter.Monocytes and Marcophages are phacocytes. Macrophages function in bothNON SPECIFIC DEFENSE (innate immunity) as well as initiate DENFENSEMECHANISIMS (Adaptive Immunity). Their role is to PHAGOCYTOSE (ENGULFand then DIGEST) cellular debris and pathogens. MARCHOPHAGE areIMPORTANT and GOOD HEALTHY CELLS Play a VERY IMPORTANT ROLE in theBODY's DEFENSE SYSTEM such as LIVER by ENGULF and then DIGEST Bacteriaand other foreign particles.

Complement in the liver is a group of protein that play a part in theIMMUNE SYSTEM's DEFENSES against INFECTION.

Due to their role in phagocytosis, Marcophages are involved in manydiseases of the IMMUNE SYSTEM. Like HIV infection, Marcophages play arole in Human Immunodeficiency Virus (HIV) infection. Like T cells,macrophages can be infected with HIV, and even become a reservoir of ongoing virus replication throughout the body. Due to the LACK of GOODHEALTHY CELLS in the body; the BAD INFECTED CELLS has gone through theSystem in the LIVER and The BAD CELLS EAT THE BAD CELLS AGAIN That iswhy VIRUS REPLICATE. Our Study NAT Testing of a POSITIVE by NAT of HIV1,2 has shown the reduction of IU/ML after three days of introducing ourAFODRAAS 1 and AFCCRAAS 1 into the HIV 1,2 POSITIVE PLASMA.

HEART DISEASE: Marcophages are the predominant cells involved increating the PROGRESSIVE PLAQUE LESIONS of ARTHEROSCLEROSIS. That is whylowering down Triglycerides, VLDL, LDL, and increasing HDL WILL NOTREMOVE THE PLAQUE LESIONS by a FOREIGN SUBSTANCES like CHEMICALS that DONOT CONTAIN a GOOD HEALTHY MARCOPHAGE CELL or Some other GOOD HEALTHYCELLS which have not been discovered as We have seen a lot more ofproteins found in Fraction III of plasma under investigation. In ourstudy of 52 Rabbits has proven this.

TUBERCULOSIS: Once engulfed by a macrophage the causative agent oftuberculosis, Mycobacterium tuberculosis avoids cellular defenses anduses the cell to replicate.

CANCERS:

Macrophages are believed to help cancer cells proliferate as well. Theyare attracted to oxygen-starved (hypoxic) tumor cells and promotechronic inflammation. Inflammatory compounds such Tumor necrosis factor(TNF)released by the macrophage activates the gene switch nuclear factor−kappa B.NF-kB then enters the nucleus of a tumor cell and turns onproduction of PROTEINS that stop apoptosis and promote cellproliferation and inflammation.

For all 8 Different cancer cells line, we have tested; All Cancer Cellshave been EATEN UP to some degree at 2% protein and completely at 10%Protein.

INVENTION:

All of the following invented method of manufacturing and purification,the final product of which should contain one of the following goodcells: NEUTHROPHIL, LYMPHOCITE, EOSINOPHIL, BASOPHIL, and MARCOPHAGE

-   -   1. Manufacturing and Purification of Complex of protein found in        Fraction IV to make        -   A separated (HDL) ApoA1        -   Transferrin,        -   Alpha 1 Anti Strepsin (A1AT).    -   2. A Combined Apo/Transferrin/Human Albumin/A1 AT,    -   3. A Combined Apo Transferrin/Human Albumin, ImmunoGlobulin    -   4. A combined Apo Alpha 1 Anti Strepsin (AT1A) Human Albumin and        ImmunoGlobulin    -   5. A Manufacturing and Purification of Prothrombin Complex        Concentrated from Fibrinogen        -   That contains A1AT, Apo, Fibrinogen, Human Albumin,            Immunoglobulin.    -   6. Manufacturing and Purification of Thrombin Complex        Concentrated from Fraction III (ProthoRAAS®)        -   Containing Factor II, VII, IX, X, Transferrin, Human            Albumin, ATA1 and Apo.    -   7. Manufacturing and Purification of Complex of protein found in        Fraction III (Combined) Consisting all 13 factors, PCC,        Thrombin, AT-III, A1AT, HDL, and other NEW proteins (under        study) found in this Fraction III.    -   8. Combination of one of the above method of manufacturing and        purification of the existing line of products 1. Human Albumin        (AlbuRAAS®) Intravenous Immunoglobulin. 2. GammaRAAS®. Factor        VIII (3 HemoRAAS®) 4. Prothrombin Complex Concentrate        (ProthoRAAS®) 5. Fibrinogen (FibroRAAS®) 6. High Concentrate        Fibrinogen (FibrinGluRAAS®) 7. Thrombin (ThrombiRAAS). 8.        Thrombin for Fibrin Sealant (FibrinGluRAAS®), Hepatitis B        Immunoglobulin (Hepa B RAAS).

Any of the single protein or combined protein of the above that containsany of one of good cells namely Neutrophil, Lymphocyte, Eosinophil,Basophil and MARCOPHAGE and it is possible That new cells may be foundas we have found a lot more of Protein in the Fraction III of plasmaunder investigation.

Through in vitro and in Vivo studies have proven their potentialabilities to Kill (or Eat up) all cancer cells, bacteria, Envelopedviruses Eat up all High FAT (Triglyceride) Build up in PLAQUE. The aboveHealthy Good tissue factor cells surrounding the blood vessels in theprotein will take away, TOXICITY, BACTERIA, FAT to transform Blood IntoCLEANER (Good Blood) then go through the Filtration of the liver fromwhere The bad FAT will Go through Kidney to eliminate liquid waste asurea which comes out of our body as Urine.

Urine has been used to make UROKINASE for the treatment of stroke.

In addition, Urea fertilizer has been used for years in order to killall worms, insecticides, buds in the soil to fertilize the soil forgrowing rice, vegetables, fruits. When I was 5 years old in a poorcountry side village in Vietnam I wondered why my grandmother asked meto urinate in a jar then later my grandmother used my urine and others'as well to mix with water and fertilized the soil to grow vegetables andfruits.

In the study of 52 Rabbits, we have seen Weight losses of studiedrabbits with the control group with 10.00% weight reduction for treatedgroup 1 and 14.52% for treated group 2. Both groups were fed with HighFAT Diet. So the control of OBESITY is possible. Total Triglyceride is−3.07%, Total Cholesterol −30.07% and −37.05% VLDL-C −44.42% and −41.87%LDL-C −21.59% and −33.96% HDL 92.36%, 54.15% TC/HDL-C −55.55% and−40.48% Potential applications for all cardiovascular diseases.

Fat build up in Plaque area have been decreased 38.43 and 29.05% tocompare with control group

−27.36 −20.69 Potential applications for Stroke, Heart attack, Paralysisdue to Stroke, Blood Pressure, Hypertension.

Liver Index of the study did not show any changes after AFODRAAS 1treatment proves that the potential protein will not cause any damage tothe liver it is easy to understand that as this protein is from MotherNature, Human plasma, not from a foreign substance, chemicals thatusually react and damage the liver.

As any one guess there are 10 billion antibodies and at least 1 Trillioncells in a human body, so far circa Three hundred antibodies have beendiscovered and how many proteins have been discovered from human plasma?

Back to 1975 until now, we have discovered Hepatitis B Virus (HBV) in1975, HIV (Human Immunodeficiency virus in 1983, Hepatitis C Antibodyvirus (HCV) in 1990, Creutzfeldt-Jakob Disease prion (CJD), VariantCreutzfeldt-Jakob disease prion (v-CJD) in 2000. SARS-CoV (Severe AcuteRespiratory Syndrome corona virus 2004, West Nile Virus (WNV) in 2005,Bird Flu virus (H1N5) in 2005 Influenza A virus subtype H1N1 in 2010

Since 1975 when Hepatitis B Surface Antigen by RIA was introduced byAbbott Laboratories Even utilizing Test kit to test for the unit ofplasma for the presence of Hepatitis B Surface Antigen, Blood Productswere still CONTAMINATED with Hepatitis B virus in the products ofFibrinogen, Factor VIII, Factor IX as the Test method is not sensitiveenough. It is proven in our table for the number of Units of plasma havebeen tested by ELISA FALSE POSITIVE, but we have To use as it a QuickTesting Method to eliminate the potential donors.

For HIV virus, It was not discovered until 1984 and the method ofeffective virus inactivation by S/D discovered by New York Blood centerin mid 1985, Almost all hemophiliacs have been contaminated with HIV 1virus.

With regard to Hepatitis C Virus (HCV) was discovered in 1990 and theEnzyme linked Assay for the detection of Hepatitis C Antibody wasintroduced thereafter However, the contamination of Hepatitis C inImmuno Globulin too place in Brazil.

With regard to Hepatitis A, a non enveloped virus which cannot be killedby Solvent Detergent method Contaminated in Factor VIII in manycountries in Europe.

From 2000 on with more effective measures taken in the inactivation ofNon enveloped and Enveloped virus including prion has improvedsignificantly and with the assistance of NAT Testing's of Pool of Plasmaused for the production of Plasma derived medicinal products.

However in 2010, The Immunoglobulin of one company in Europe has causedheart attack and stroke to the patients due to their processes tooptimize yield which carries other fraction like Fraction III whichcontains Thrombin to cause Thrombosis in patients. Otherwise TodayPlasma derived medicinal products are much safer than before the year of2000.

-   -   HBV (Hepatitis B virus) 1975    -   HIV (Human immunodeficiency virus (1983)    -   HCV (Hepatitis C virus) 1990    -   CJD (Creutzfeldt-Jakob Disease prion)    -   v-CJD (Variant Creutzfeldt-Jakob Disease prion) 2000    -   SARS-CoV (Severe Acute Respiratory Syndrome corona virus) 2004    -   WNV (West Nile virus) 2005    -   H1N5 (Bird Flu virus)    -   Influenza A virus subtype H1N1 2010

For Viruses: In NAT testing of samples of HIV Positive Plasma mixed withdifferent dosages of AFODRAAS1 and AFCCRAAS 1 by NAT Testing show atremendously decrease in IU/ML. Potential killing HIV 1,2 Virus andother Enveloped and Non envelope Viruses as well.

We have made improvement in preventing the contamination of viruses intoplasma derived medicinal products, however the contamination of HumanAlbumin in 1996 in The United States with BACTERIA.

Bacteria Contamination will not spare any products. We thought when wecame up with rDNA Factor VIII, the contamination of viruses notpossible, however in 2003, the contamination of RDNA Factor VIII by oneCompany in the United States of America has caused a severe shortage ofRDNA Factor VIII in the world in 2003 and 2004.

Bacteria Contamination in Flu Vaccine in England 2004

In 2010, Bacteria contamination in Drugs in the United States of America

In 2010, Contamination of eggs (substrate for vaccine production) withSalmonella enteritidis.

-   -   Recombinant DNA products like rDNA Factor VIII in 2003    -   Vaccine in 2004 (England)    -   Contamination of eggs (substrate for vaccine production) with        Salmonella enteritidis (2010)

For Bacteria:

For both AFODRAAS 1 and AFCC RAAS1 have killed some kind of lethalBacteria like Staphylococcus aureus that are resistant to our currentantibiotic arsenal MARSA (Methicillin-Resistant Staphylococcus aureuswhich currently kill approximately 20,000 people a year in the USaccording to Forbes Feb. 14, 2011. Potential indications for allbacteria and SEPSIS which kill about 200,000 people a year in US out of700,000 people having SEPSIS with LARGE dosages.

The contamination of Bacteria SHOULD NOT HAPPEN in FIRST PLACE, howeverAny Drugs combined with AFODRAAS1-85 and AFCCRAAS1-85 with LARGE DOSAGEwill prevent BACTERIA Contamination.

For Solid Tumor cancers and Blood (Liquid) Cancers: A total of 8different cells for Colon cancer cell Hct-116, Colon cancer line LS174T,Breast Cancer cell MCF-7, Liver cancer cell HepG2, Pancreas Cancer cellPAC-1 Gastric Cancer cell 7901, Gastric Cancer cell AGS, and Gastriccancer line with 2000 cell each type were used to test with 2% ofprotein which killed certain number of cancers cells big number orsmaller number depending type of cells but at 10% protein All abovecancer cells are KILLED. Potential applications for all solid tumorcancers and blood (liquid) cancers.

All of diseases, cancers, inhibitors, Immune deficiencies are caused byBAD CELLS which turn into the bacteria, viruses, prion.

Now with this invention, we can conclude due to the lack of healthycells which are in the blood going through liver for manufacturing,moderating, regulating, and distributing to the other organs and otherparts of our body, such as brain (due to the lack of these healthycells, people having Alzheimer/Autism/Parkinson)

For Diabetic due to accumulation of Glucose (which is also FAT) withthese Healthy cells can eat Up all FAT and send Good blood cells tokidney to help produce INSULIN.

For Hemophiliac A, B and VwB One of the liver function is to produceCoagulant, however these Hemophiliac lack Good HEALTHY Cells for theliver to produce Coagulant.

All Good Healthy cells from Protein which is also produced by Liver canprevent the production of Endotoxin (Transferin), cytokine, toxicity,TNF and prevent the activation of HISTONE.

All Good Healthy cells from Protein or Antibodies which is also producedby the Liver can prevent all of deficiencies in our bodies.

All Good Health cells from Protein or Antibodies can be used with otherdrugs currently in the market or in the future to prevent side affectsdamaging the liver, kidney or any other organs of the body along withheart attack like in the case of Viagra, and work much better with DrugsTo lower Triglycerides like Arvostatin and Lipitor for decreasing LDL.These are well known drugs not to mention, it will work well with otherthousands of drugs available in the market today and And any futuredeveloped drugs

Background

The liver is the ONLY ORGAN which produces PROTEINS and ANTIBODIES, bothof which play a very important roles in the defense of people againstdiseases, viruses, bacteria infections. This discovery reveals anyprotein that contains A GOOD HEALTHY CELL will properly can be usedagainst Any diseases, viruses, bacteria, deficiencies, inhibitors, prionin our body and thus from now on mankind will be protected Against allkinds of diseases, cancers, epidemics, viruses, bacteria and possiblyblind, deaf, mute people may benefit.

The Cells of the blood can be divided into: white blood cells, red bloodcells and platelets.

Red blood cells, or erythrocytes are the most common type of blood celland our principal means of delivering oxygen to the body tissues throughthe circulatory system (arteries). Red blood cells take up oxygen in thelungs and release it while circulating through the body's capillaryvessels (the smallest structures that conduct blood), where they take upcarbon dioxide, which is a waste product of metabolism, and take it tothe lungs, to be discarded through the respiration. These cells are richin hemoglobin, which is a molecule that contains iron and that can bindoxygen (and is responsible for the blood's red color).

The red blood cells develop in the bone marrow and circulate for about100-120 days in the body before their components are recycled bymacrophages.

Red blood cells do not participate in the immune system.

Platelets are cell fragments (that is, cells that do not have a nucleus,2-3 μm in diameter, which are derived from fragmentation of precursorcells known as “megakaryocytes”.

The average lifespan of a platelet is normally just 5 to 9 days.Platelets play a fundamental role in hemostasis with the formation ofclots, but they do not participate in the immune system.

White blood cells, or leucocytes, are cells of the immune systeminvolved in defending the body against both infectious disease andforeign materials. There are five different and diverse types ofleukocytes exist, but they are all produced and derived from a multipotent cell in the bone marrow, known as a hematopoietic stem cell.Leukocytes are found throughout the body, not only in the blood and thelymphatic system.

The number of white blood cells in the blood is often an indicator ofdisease. There are normally between 5'000 to 10'000 white blood cellsper mL. An increase in the number of leukocytes over the upper limits scalled leukocytosis, and a decrease below the lower limit is calledleukopenia.

Type of cell % Main targets Lifetime Neutrophil 54-62 Bacteria and fungi6 hs to a few days Lymphocyte 25-33 B Lymphocytes (releases antibodiesand Weeks to assist “activation” of T lymphocytes) years T Lymphocytes:Helper (activate and regulate T and B lymphocytes) Cytotoxic Tlymphocytes CD8+ (virus- infected and tumor cells) Gamma-delta Tlymphocytes (suppressor T lymphocytes) Returns the functioning of theimmune system back to normal operation after infection and preventsautoimmunity Natural killer T lymphocytes (virus- infected and tumorcells) Eosinophil 1-6 Larger parasites 8-12 days Modulate allergicinflammatory responses Basophil <1 Release mediators (histamine) Hoursto in inflammatory response days Monocyte  2-10 Monocytes migrate fromthe Hours to bloodstream to other tissues and days differentiate intotissue resident macrophages or dendritic cells Macrophage No*Phagocytosis (engulfment and activated: digestion) o fcellular debrisand days pathogens, and stimulation of immature: lymphocytes and otherimmune cells months to that respond to the pathogen. years

Another important support role in transporting protein is Chylomicrons(Mainly Triglycerides which is considered very BAD according to a lot ofpublications and it may lead to Heart attack and Stroke. However,without triglycerides FATS and cholesterol cannot Move within thewater-based solution of the Blood stream.

Chylomicrons are large lipoprotein particles that consist oftriglycerides (85-92%), phospholipids (6-12%), cholesterol (1-3%) andproteins (1-2%) [1]. They transport dietary lipids from the intestinesto other locations in the body. Chylomicrons are one of the five majorgroups of lipoproteins (chylomicrons, VLDL, IDL, LDL, HDL) that enablefats and cholesterol to move within the water-based solution of thebloodstream.

Function: Chylomicrons transport exogenous lipids to liver, adipose,cardiac, and skeletal muscle tissue, where their triglyceride componentsare unloaded by the activity of lipoprotein lipase. As a consequence,chylomicron remnants are left over and are taken up by the liver.

Origin

Chylomicrons are a type of lipoprotein produced in absorptive cells ofsmall intestines, specifically, the epithelial cells within the villi ofthe duodenum.

Stages

There are three stages in the chylomicron's “life cycle”:

Nascent chylomicron

Mature chylomicron

Chylomicron remnant

Nascent Chylomicrons

Chylomicrons are created by the absorptive cells of the small intestine,known as enterocytes. They are relatively large, having a diameter of 75to 1,200 nm. These nascent chylomicrons are released by exocytosis fromenterocytes into lacteals, lymphatic vessels originating in the villi ofthe small intestine, and are then secreted into the bloodstream at thethoracic duct's connection with the left subclavian vein.

Nascent chylomicrons are primarily composed of triglycerides (85%) andcontain some cholesterol and cholesteryl esters. The main apolipoproteincomponent is apolipoprotein B-48 (APOB48).

Mature Chylomicron

While circulating in lymph and blood, chylomicrons exchange componentswith high-density lipoproteins (HDL). The HDL donates apolipoproteinC-II (APOC2) and lipoprotein E (APOE) to the nascent chylomicron andthus converts it to a mature chylomicron (often referred to simply as“chylomicron”). APOC2 is the cofactor for lipoprotein lipase (LPL)activity.

Chylomicron Remnant

Once triglyceride stores are distributed, the chylomicron returns APOC2to the HDL (but keeps APOE), and, thus, becomes a chylomicron remnant,now only 30-50 nm. APOB48 and APOE are important to identify thechylomicron remnant in the liver for endocytosis and breakdown.

References1.̂ M Mahmood Hussain: “Review Article: A proposed model forthe assembly of chylomicrons”; Arterosclerosis; Vol. 148; 2000; pages1-15;

INVENTIONS: Several Manufacturing processes of a protein that containone of the Healthy GOOD CELLS as described. Few of them are describedhere and the rest as we can separate Protein by Protein by differentprocess, it can be combined from one protein with others to contain oneof these Health Good Cells.

The present invention relates to a method of introduction of a healthygood human cells to eat up bad damaged or cells, comprisingadministering an effective amount of a healthy good protein containingtransferin, alpha 1-antitrypsin, apolipoprotein A and human albumin.

By the present invention, damage to healthy human cells can be reducedby administering an effective amount of a healthy good proteincontaining ApoA1/2/4 and/or transferrin and/or alpha 1 antitrypsinand/or C1 esterase inhibitors and other inhibitors.

The present invention also involves a method of introduction of healthygoodies human cells to eat up bad damaged cells to reduce damage tohealthy human cells, comprising administering an effective amount of ahealthy good protein containing Factor II, Factor VII, Factor IX andFactor X in Prothrombin Complex Concentrate (ProthoRAAS®). The damage tohealthy human cells can be reduced by administering an effective amountof a protein containing any one or more of: human albumin (AlbuRAAS®),immunoglobulin (GammaRAAS®), fibrinogen (FibroRAAS®), Factor VIII(HemoRAAS®), high concentrate fibrinogen (FibrinGluRAAS®), thrombin(ThrombiRAAS®), Hepatitis B and Immune Globulin (HBIG) (HepaRAAS®).

The present invention further involves a method of reducing damage tohealthy human cells, comprising administering an effective amount of ahealthy good protein containing one or more of: Anti thrombin III(AT-III), protein C, fibronectin, protein S, and protein M. An effectiveamount of two or more of the proteins described herein for use with thepresent invention can be used. The proteins include all currently knownproteins and proteins yet to be discovered in Fraction III of plasma.

The method of the present invention further involves reducing damage tohealthy human cells by administering an effective amount of any of: amacrophage, a neutrophil, a basophil, a lymphocyte and an eosinophil inwhite blood cells, red blood cells, platelets, chylomicrons,electrolyses, and peptides in humans or in animals or in chemicals or insubstances from any source of materials obtaining by clone expressing toobtain the cells for further purification by rDNA, monoclonal,transgenic, or by any other methodology.

The more healthy good proteins that are used in effective amounts in acombination of proteins means that the combination will be more potentand effective than a single healthy good protein in the treatment ofdiseases and viruses or bacterial infections. The method of reducingdamage to healthy human cells according to the present inventioncomprises any good healthy protein of, for example, AFOD RAAS 1-85 andAFCC RAAS 1-85 can be combined with any currently available and futuredeveloped drugs to enhance the efficacy, while reducing toxicity and theside effects caused by chemical drugs.

The method according to the present invention also involves introducinghealthy goodies human cells to eat up bad damaged cells, the methodcomprising administering an effective amount of a protein containing atleast one of the following apolipoproteins: ApoA1, ApoA2, ApoA4,Apo-B48, ApoB100, ApoCI, ApoCII, ApoCIII, Apo-D, Apo-E, Apo-H, andApo(a), all of which contain good healthy cells. The protein furthercontains at least one of the following: alpha 1 antitrypsin (A1AT),transferrin, and human albumin, all of which contain good healthy cells.

BRIEF DESCRIPTIONS OF THE DRAWING FIGURES

FIG. 1 is a flowchart of a process of purifying APO from plasma fractionIV according to the present invention;

FIG. 2 is a flowchart of another process of purifying APO from plasmafraction IV according to the present invention;

FIG. 3 is a flowchart of an AFCC process of purifying prothrombincomplex from cryopaste in accordance with the present invention;

FIG. 4 is a flowchart of an AFCC process of purifying prothrombincomplex from fraction III in accordance with the present invention;

FIG. 5 shows the electrophoresis result of cation chromatography ofproteins including transferrin, human albumin, APOA1, PCC and A1AT;

FIG. 6 shows the 2D electrophoresis results of AFOD;

FIG. 7 shows an analysis of a Fraction IV suspension by 2Delectrophoresis;

FIG. 8 is a graph showing the relative abundance over time of Q8 GeneSymbol=GC Vitamin D binding protein Precursor—Cask isoform 3 ofPeripheral plasma membrane potein CASk—VIM Vimentin;

FIG. 9 is a graph showing the relative abundance over time of Q13 GeneSymbol=CASK Isoform 3 of Peripheral plasma membrane protein CASK—HP HPprotein;

FIG. 10 is a graph showing the relative abundance over time of Q15 GeneSymbol—CASK Isoform 3 of Peripheral plasma membrane protein CASK—IFNA13IFNA1 Interferon alpha-1/13;

FIG. 11 shows the results of a 2D electrophoresis of prothrombin complexconcentrate;

FIG. 12 shows the results of a 2D electrophoresis of Fraction III;

FIG. 13 shows the results of a 2D electrophoresis of cryopaste;

FIG. 14 is a flowchart of a process for purifying AFOD;

FIG. 15 is a graph showing cancer cell proliferation during a 3-day invitro study of colon and breast cancer cell lines in the presence ofvarying concentrations of AFOD solution;

FIG. 16 is an image taken on Day 3 after treatment showing theproliferation of Colon cancer cells HCT 116 in 0% AFOD solution;

FIG. 17 is an image taken on Day 3 after treatment showing theproliferation of Colon cancer cells HCT 116 in 2% AFOD solution;

FIG. 18 is an image taken on Day 3 after treatment showing theproliferation of Colon cancer cells HCT 116 in 10% AFOD solution;

FIG. 19 is an image taken on Day 3 after treatment showing theproliferation of Breast cancer cells MCF-7 in 0% AFOD solution;

FIG. 20 is an image taken on Day 3 after treatment showing theproliferation of Breast cancer cells MCF-7 in 2% AFOD solution;

FIG. 21 is an image taken on Day 3 after treatment showing theproliferation of Breast cancer cells MCF-7 in 10% AFOD solution;

FIG. 22 is a graph showing cancer cell proliferation during a 3-day invitro study of liver and pancreas cancer cell lines in the presence ofvarying concentrations of AFOD solution;

FIG. 23 is an image taken on Day 3 after treatment showing theproliferation of liver cancer cells HepG2 in 0% AFOD solution;

FIG. 24 is an image taken on Day 3 after treatment showing theproliferation of liver cancer cells HepG2 in 2% AFOD solution;

FIG. 25 is an image taken on Day 3 after treatment showing theproliferation of liver cancer cells HepG2 in 10% AFOD solution;

FIG. 26 is an image taken on Day 3 after treatment showing theproliferation of pancreas cancer cells PAC-1 in 0% AFOD solution;

FIG. 27 is an image taken on Day 3 after treatment showing theproliferation of pancreas cancer cells PAC-1 in 2% AFOD solution;

FIG. 28 is an image taken on Day 3 after treatment showing theproliferation of pancreas cancer cells PAC-1 in 10% AFOD solution;

FIG. 29 is a graph showing the proliferation of a variety of cancercells over a 3-day trial period in the presence of varyingconcentrations of AFOD;

FIG. 30 shows the images of FIGS. 16-21 next to one another forcomparison;

FIG. 31 shows the images of FIGS. 23-28 next to one another forcomparison;

FIG. 32 is a graph showing cell proliferation during a 3-day in vitrostudy of cervical cancer cell line Hela in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 33 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Cervical Cancer line Hela in the presence of 16different solutions (listed on each photo). The solutions are CK, HA10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 34 is a graph showing cell proliferation during a 3-day In Vitrostudy of Gastric cancer cell AGS in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 35 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Gastric Cancer Cell AGS in the presence of 16different solutions (listed on each photograph). The solutions are CK,HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 36 is a graph showing cell proliferation during a 3-day In Vitrostudy of Breast Cancer Cell Line SK-BR-3 in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 37 contains 9 photos taken on Day 3 after treatment, showing theproliferation of Breast Cancer Cell Line SK-BR-3 in the presence ofdifferent solutions (listed on each photograph). The solutions are CK,HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB25 U/mL, and TB 5 U/mL;

FIG. 38 contains 7 photographs taken on Day 3 after treatment, showingthe proliferation of Breast Cancer Cell Line SK-BR-3 in the presence ofdifferent solutions (listed on each photograph). The solutions are AFCC33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD0.5%. and AFOD 0.1%;

FIG. 39 is a graph showing cell proliferation during a 3-day In Vitrostudy of Ovarian Cancer Cell Line SK-OV-3 in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 40 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Ovarian Cancer Cell SK-OV-3 in the presence of 16different solutions (listed on each photograph). The solutions are CK,HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 41 is a graph showing cell proliferation during a 3-day In Vitrostudy of Lung Adenocarcinoma Cell Line SPC-A-1 in the presence of 16distinct solutions, listed on the x axis. The solutions are CK, HA 10%,HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL,TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL,AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 42 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Lung Adenocarcinoma Cell Line SPC-A-1 in thepresence of 16 different solutions (listed on each photograph). Thesolutions are CK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL,HemoRAAS 5 U/mL, TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL,rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 43 is a graph showing cell proliferation during a 3-day In Vitrostudy of Espohageal Cancer Cell Line TE-1 in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 44 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Espohageal Cancer Cell Line TE-1 in the presence of16 different solutions (listed on each photograph). The solutions areCK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL,TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 45 is a graph showing cell proliferation during a 3-day In Vitrostudy of Liver Cancer Cell Line BEL-7402 in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 46 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Liver Cancer Cell Line BEL-7402 in the presence of16 different solutions (listed on each photograph). The solutions areCK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL,TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 47 is a graph showing cell proliferation during a 3-day In Vitrostudy of Pancreas Cancer Cell Line PANC-1 in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 48 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Pancreas Cancer Cell Line PANC-1 in the presence of16 different solutions (listed on each photograph). The solutions areCK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL,TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 49 is a graph showing cell proliferation during a 3-day In Vitrostudy of Leukemia Cancer Cell Line Dami in the presence of 16 distinctsolutions, listed on the x axis. The solutions are CK, HA 10%, HA 2%,IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL, TB 25 U/mL, TB 5U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII 15 U/mL, AFOD2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 50 contains 16 photographs taken on Day 3 after treatment, showingthe proliferation of Leukemia Cancer Cell Line Dami in the presence of16 different solutions (listed on each photograph). The solutions areCK, HA 10%, HA 2%, IVIG 10%, IVIG 2%, HemoRAAS 25 U/mL, HemoRAAS 5 U/mL,TB 25 U/mL, TB 5 U/mL, AFCC 33 U/mL, AFCC 6 U/mL, rFVIII 65 U/mL, rFVIII15 U/mL, AFOD 2.5%, AFOD 0.5%. and AFOD 0.1%;

FIG. 51 is a graph showing the summary data for the proliferation ofLeukemia Cells (Acute Promyelocytic Leukemia Cell T24) in the presenceof 0% protein, 2% protein, and 10% protein of AFOD, and Bladder Cancercells (Bladder Cancer Cell NB4) in the presence of 0% protein, 2%protein, and 10% protein of AFOD during the 3-day trial period.

FIG. 52 shows 6 pictures taken after the trial which show theproliferation of Leukemia Cells (Acute Promyelocytic Leukemia Cell T24)in the presence of 0% protein, 2% protein, and 10% protein of AFOD, andBladder Cancer cells (Bladder Cancer Cell NB4) in the presence of 0%protein, 2% protein, and 10% protein of AFOD during the 3-day trialperiod.

FIG. 53 is a graph showing the summary data for the proliferation ofCervical Cancer Cells (Human Cervical Cancer Cell Line Hela) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 54 is a graph showing the summary data for the proliferation ofGastric Cancer Cells (Human Gastric Cancer Cell Line AGS) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 55 is a graph showing the summary data for the proliferation ofOvarian Cancer Cells (Human Ovarian Cancer Cell SK-OV-3) in the presenceof a variety of solutions, listed on the x-axis, at 0%, 2%, and 10%concentrations of protein, respectively.

FIG. 56 is a graph showing the summary data for the proliferation ofBreast Cancer Cells (Human Breast Cancer Cell Line SK-BR-3) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 57 is a graph showing the summary data for the proliferation ofEsophageal Cancer Cells (Human Esophageal Cancer Cell Line TE-1) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 58 is a graph showing the summary data for the proliferation ofLiver Cancer Cells (Human Liver Cancer Cell Line BEL-7402) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 59 is a graph showing the summary data for the proliferation ofLung Cancer Cells (Lung Adenocarcinoma Cell Line SPC-A-1) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 60 is a graph showing the summary data for the proliferation ofPancreas Cancer Cells (Human Pancreas Cancer Cell Line PANC-) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 61 is a graph showing the summary data for the proliferation ofLeukemia Cells (Human Lymphocyte Leukemia Cell Line Jurkat) in thepresence of a variety of solutions, listed on the x-axis, at 0%, 2%, and10% concentrations of protein, respectively.

FIG. 62 is a photograph of five sample vials of bacteria during amicrobe test with AFOD RAAS 1 on Staphylococcus aureus, from left toright, having 8 mL AFOD added, having 10 mL AFOD added, having 12 mLAFOD added, a positive control, and a negative control.

FIG. 63 is a series of photographs of three sample vials of bacteria,taken at different times during a microbe test of AFOD on Staphylococcusaureus.

FIG. 64 is a series of photographs of five sample vials of bacteria,taken at different times during a microbe test of AFCC on Staphylococcusaureus.

FIG. 65 is a photograph showing the aorta of a lab animal given a highfat diet after 10 weeks, with a plaque area of 24.3%.

FIG. 66 is a photograph showing the liver tissue (with fat deposits) ofa lab animal after 10 weeks of a high fat diet.

FIG. 67 is a photograph showing the aorta of a lab animal without AFODRAAS 1 and then a normal diet for 4 weeks, with a plaque area of 45.3%.

FIG. 68 is a photograph showing the aorta of a lab animal without AFODRAAS 1 and then a normal diet for 8 weeks, with a plaque area of 98.5%.

FIG. 69 is a photograph showing the aorta of a lab animal without AFODRAAS 1 and then a normal diet for 8 weeks, with a plaque area of 78.94%.

Each of FIGS. 70-76 is a photograph of a container having a mixture of aproduct with a yellow color and a product with a blue that, unlikeyellow and blue chemicals, will not turn green.

FIG. 77 is a photograph showing an artery of a lab animal is given anormal diet for 8 weeks.

FIG. 78 is a photograph showing the aortas of two lab animals tested byAFOD RAAS 1, the aortas having a plaque area of 0.

FIG. 79 is a photograph showing the buildup of plaque to a plaque areaof 13.29% in the aorta of a lab animal with AFOD RAAS 1-A1 for 8 weeks.

FIG. 80 is a photograph showing the buildup of plaque to a plaque areaof 20.5% in the aorta of a lab animal with AFOD RAAS 1-A1 for 8 weeks.

FIG. 81 is a photograph showing the buildup of plaque to a plaque areaof 58.4% in the aorta of a lab animal with AFOD RAAS 1.

FIG. 82 is a photograph showing the buildup of plaque to a plaque areaof 82.17% in the aorta of a lab animal with AFOD RAAS 1.

FIG. 83 is a photograph showing the buildup of plaque to a plaque areaof 47.27% in the aorta of a lab animal with AFOD RAAS 1 for 11 weeks.

FIG. 84 is a photograph showing the buildup of plaque to a plaque areaof 40.32% in the aorta of a lab animal with AFOD RAAS 1 for 11 weeks.

FIG. 85 is a photograph showing the buildup of plaque to a plaque areaof 51.13% in the aorta of a lab animal with AFOD RAAS 1 for 11 weeks.

The 3^(rd) generation of APO purification.

The main difference is that urea is no longer required but need 2 stepsof chromatography, as is shown in FIG. 1.

-   1. A method to purify APO from plasma fraction IV,    -   1) Fraction IV is resuspended in a buffer with pH 3.00-10.00,        and the celite and other impurities were separated by press        filter or centrifugation, the resulted supernatant was then        collected,    -   2) The APO in the supernatant was then precipitated by adding        NaCl and then was spin to collect the paste,    -   3) The resulted APO was then resuspended and filtered,    -   4) The resulted suspension was then underwent DEAE ion        exchanging chromatography and butyl chromatography,-   2. the fraction IV was resuspended in NaAc buffer with pH 3.00-10.00-   3. the APO was precipitated by NaCl, pH 3.0-10.0, cool down to −1 to    10-   4. the paste of APO can be resuspended in WFI or NaCl solution with    pH 3.00-10.00 and 0-10 C-   5. The resulted suspension is filtered with 0.45 um filter.-   6. The chromatography in step 4 is Canion (DEAE) and butyl-   7. The purification of APO by chromatography compromising,    -   Canion chromatography, adjust pH of filtered APO suspension to        3.0-10.0 and ionic strength to 15-25 mM, load on DEAE        chromatography, low salt wash the DEAE chromatography, and then        high salt elute the DEAE chromatography, collect the resulted        APO elute,    -   Butyl chromatography, the resulted APO elute from DEAE        chromatography is adjusted to pH 3.0-10.0 and low salt wash for        impurities, WFI or alkaline buffer wash to collect APO enriched        elute-   8. The low salt buffer is a buffer containing Tris with pH    3.00-10.0, the high salt buffer is a buffer containing NaCl, the low    salt elute buffer is a buffer containing Tris, the alkaline buffer    is a buffer containing NaOH with pH 3.0-10.0-   9. The resulted high purity of APO is then dialyzed and concentrated    with virus inactivation, adding stabilizer and lyophilized.

PROCESS Nr 4.

A process that is separated the Fraction IV into 4 Proteins, as can beappreciated from FIG. 2:

1. Transferrin 2. Human Albumin 3. APO 4. Alpha 1 Anti Strepsin (A1AT)5. Transferrin+Human Albumin+APO+Immunoglobulin 6. HumanAlbumin+APO+Alpha 1 AntiStrepsin (A1AT)+Immunoglobulin 7. HumanAlbumin+APO+Immunoglobulin 8. HumanAlbumin+APO+Immunoglobulin+Transferrin+AntiStrepsin.

Or all products from Nr 5 to Nr 8 can be processed separately and puttogether at the Non Sterile Final Bulk—Sterile Filtration-Filling—FinalProducts.

1. Re suspension of fraction IV and pretreatment1) Fraction IV is resuspended in a buffer with pH 3.00-10.00,2) The celite and other impurities were separated by press filter ofcentrifugation; the resulted suspension was then collected,3) The suspension was then treated with SD virus inactivation,4) The resulted suspension was then subject to a canion chromatographylike DEAE,5) Proteins were eluted in different fractions,6) The different eluted fractions were then further purified,2. The fraction IV was dissolved in low temperature buffer to achieve ain homogenous suspension,3. The celite in resulted suspension can be removed by press filter orcentrifugation,4. the suspension was then cleared by depth filter5. the resulted suspension was then treated with Tween-80 and TNBP forvirus inactivation at 25 C for 6 hours,6. The resulted suspension was adjusted pH and ionic strength and thensubjected to a canion chromatography like DEAE. The targeted proteinswere then binding to the canion chromatography resin, which aretransferrin, human albumin, APO and A1AT. The 1^(st) elution was saltsolution to elude the transferrin. The 2^(nd) elution was then eluded bya high concentration salt solution, which was APO. The 3^(rd) elutedfraction was human albumin by a low pH solution. Finally the 4^(th)elution was A1AT which was eluted by a high concentration salt solution.7. The resulted various elution was then subjected to differentchromatography for further purification to achieve a high purity. The1^(st) elution fraction was subjected to a CM chromatography. The 2^(nd)elution fraction was subjected to a butyl chromatography.

The 3^(rd) elution fraction was subjected to a blue chromatography. The4^(th) elution fraction was subjected to a blue chromatography and asubsequent butyl chromatography.

8. The resulted protein fractions were then dialyzed and concentrated.The pH was adjusted and stabilizer was then added.9. The resulted protein solutions were subjected to DV20 filtration forvirus removal except human albumin.10. The human albumin could be virus inactivated by Doublepasteurization.11. The resulted transferrin, APO, human albumin and A1AT can be filled.

AFCCRAAS 1: These processes of protein containing Healthy Good cells inProcess 1 and Process 3 below are specially designed for Hemophilia A,Band WvB who have Been infected by HBV, HCV and specially HIV during theearly of 1980 when effective process of inactivation of Envelopedviruses has not been introduced.

1. Process to separate Factor II, VII, IX, and X Transferrin, HumanAlbumin, APO and A1AT (ProthoRAAS®) from fraction III which also containat least 20 ADDITIONAL PROTEINS which are BEING DISCOVERED.2. Process to separate Factor II, VII, IX, and X (ProthoRAAS®)+HumanAlbumin (AlbuRAAS®)+Immunoglobulin (GammaRAAS)3. Process to separate Factor II, VII, IX and X from Cryopaste4. Process to separate Factor II, VII, IX and X from Cryopaste+ATA1APO+Human Albumin (AlbuRAAS®) and Immunoglobulin (GammaRAAS)5. Process to separate Thrombin (ThrombiRAAS®) from Fraction III6. Process to combine all protein from Fraction III.

Description

-   -   1. As can be seen in FIG. 3, this process describes a process to        purify prothrombin complex from cryoprecipitaiton, which        comprises,    -   1) Re-constitute cryopaste in buffer containing 3,000 U/kg        heparin,    -   2) Adjust pH and temperature    -   3) Complete mix at room temperature for 3 to 5 hours    -   4) Filter the resulted suspension with 10CP+90SP filter    -   5) Solvent detergent virus inactivation of resulted suspension    -   6) weak anion exchange chromatography of SD virus inactivated        suspension    -   7) Twice washing of weak anion exchange chromatography    -   8) Elute weak anion exchange chromatography 2 to 3 times    -   9) Collect the result elution and ultra-filter with 10K membrane    -   10) Adjust pH of resulted elution    -   11) Adjust the activity of human FIX in the resulted elution    -   12) Aseptic filtration and nano filtration for virus removal    -   13) Filling and lyophilization

Description

-   -   2. As can be seen in FIG. 4, this process describes a process to        purify prothrombin complex from fraction III, which comprises,    -   14) Re-constitute cryopaste in buffer,    -   15) Adjust pH and temperature    -   16) PEG precipitation of resulted fraction III suspension    -   17) Centrifugation and collect the supernant    -   18) Filter the resulted suspension with 10CP+90SP filter    -   19) Solvent detergent virus inactivation of resulted suspension    -   20) weak anion exchange chromatography of SD virus inactivated        suspension    -   21) Twice washing of weak anion exchange chromatography    -   22) Elute weak anion exchange chromatography 2 to 3 times    -   23) Collect the result elution and ultra-filter with 10K        membrane    -   24) Adjust pH of resulted elution    -   25) Adjust the activity of human FIX in the resulted elution    -   26) Aseptic filtration and nano filtration for virus removal    -   27) Filling and lyophilization

AFOD is High density Lipoprotein (ApoA1):

Reference is made to FIGS. 5 and 6. The three dots in our analysis ofAFOD are all ApoA1. The difference showed in 2D electropherosis of FIG.6 might be due to different isoform of ApoA1 or Apo in the Apo family.

-   -   1. HDL (ApoA1): AFOD RAAS 1 (Trade mark) contains purified ApoA1        in the process described Nr 1 (China Patent granted        200610147503.7) Nr1 &N2 (US 2009/0286960 A1) Nr 3,4 (U.S.        61/457,380) with a purity of 96% and the products must be free        of all HIV1,2, HCV, HBV viruses and contain very good level of        High Density Lipoprotein (HDL) which is GOOD        -   CHOLESTEROL, No value or very low value of VLDL (Very low            density Lipoprotein) and no value or very low value of LDL            (Low Density Lipoprotein), both of which are BAD            CHOLESTEROL. Potential applications: Cholesterol, Angina,            hyperlipidemia, Clean plaque, fat on liver, Life span,            Control of Obesity, Hypertension, Prevention of Heart            attack, Prevention of Stroke, Prevention of Paralysis due to            the stroke and other potential indications as described.    -   2. AFODRAAS 2 (Human Albumin+ApoA1) In addition to current        clinical applications for AlbuRAAS® Potential applications for        trauma management/Arthritis/Schizophrenia/Depression/Certain        types of cancers Lung, Pancreas, Kidney, Liver, Prostate, Breast        and other potential indications    -   3. AFODRAAS 3 (Intravenous Immuno Globulin+ApoA1) for current        clinical applications for GammaRAAS® and for potential        applications for all blood (liquid) cancers as described in        abstract)    -   4. AFODRAAS 4 (Factor VIII+ApoA1) for the current clinical        applications of HemoRAAS® and for potential applications for        Hepatitis B, Hepatitis C and HIV 1,2, Bleeding        complications/Bone Surgery in Patients with Hemophilia A        (orthopedics, liver, pancreas, cancer of the gastrointestinal        tube and eventually build up Coagulation so patients will no        longer need to use Factor VIII for hemophilia A and all solid        tumor and blood cancers/    -   5. AFODRAAS5 (Prothombin Complex Concentrate+ApoA1) for the        current clinical applications of ProthoRAAS® and for potential        applications for Hepatitis B, Cirrhosis, and other hepatic        trouble like biliary tree obstruction Hepatitis C, HIV 1,2        Bleeding/Bone Complications and surgeries for Hemophilia B and        Hemophilia A with inhibitor and eventually build up coagulation        so patients will no longer need to use Factor IX or PCC and all        solid tumor and blood cancers    -   6. AFODRAAS6 (Thrombin+ApoA1) for the current clinical        applications of ThrombiRAAS® and for potential applications for        Gastric and duodenal ulcer, ulcers and other problems of colon        (large intestine)    -   7. AFODRAAS7 (Fibrinogen+ApoA1) for the current clinical        applications of FibroRAAS® and for potential applications for        Trauma Management and other potential indications as described    -   8. AFODRAAS8 (Fibrin Sealant+ApoA1) for the current clinical        applications of FibrinGluRAAS® and potential TOPICAL        APPLICATIONS for ALL SOLID TUMOR CANCERS which can be operated        and cancers have not been spread to other parts of body.    -   9. AFODRAAS 9 (ApoA1+Human Albumin (AlbuRAAS)+Alpha 1 Anti        strepsin (A1AT)+Transferrin for all potential indications as        described    -   10. AFODRAAS 10 (ApoA1+Human Albumin+Alpha 1 Anti Strepsin        (A1AT) for all potential indications as described.    -   11. AFODRAAS 11 (ApoA1+Human Albumin+Transferrin) for all        potential indications as described.    -   12. AFODRAAS 12 (ApoA1+Alpha 1 Anti Strepsin (A1AT) for all        potential indications as described.    -   13. AFODRAAS 13 (ApoA1+Transferrin for all potential indications        as described.    -   14. AFODRAAS 14 (Alpha 1 Anti Strepsin (A1AT)+Transferrin) for        all potential indications as described.    -   15. AFODRAAS 15 (Transferrin) for All potential indications as        described.

In our analysis of Fraction IV suspension by 2D electropherosis, asshown in FIG. 7, the following proteins were found in the Fraction IVsuspension:

The main proteins found in Fraction IV suspension are:

-   -   Transferrin, Human Albumin, Alpha 1 AntiStrepsin, and ApoA1

The rest of the proteins are: SEMENOGELIN-1, HAPTOGLOBIN, VIMENTIN,NESPRIN-2, INTERFERON ALPHA 1/13, HP PROTEIN, VITAMIN D-BINDING,ALPHA-FETOPROTEIN, CASK, AMYLOID PRECURSOR, NEUREXINS AND SYNDECANS.

SEMENOGELIN-1: The protein encoded by this gene is the predominantprotein in semen

HAPTOGLOBIN: In Blood Plasma, Haptoglobin binds free hemoglobin(Hb)released from erythrocytes with high affinity and thereby inhibitsits oxidative activity.

VIMENTIN is a member of the intermediate filament family of proteinsthat is especially found in connective tissue. They, along withmicrotubules and actin microfilaments, make up the cytoskeleton

THE NESPRINS are a family of proteins that are found primarily in theouter nuclear membrane. Nesprin-1 and Nesprin-2 bind to actin filaments.

VITAMIN-D BINDING PROTEIN belongs to the albumin gene family, togetherwith Human serum albumin and alpha-fetoprotein. It is a multifunctionalprotein found in plasma, ascetic fluid, cerebrospinal fluid and on thesurface of many cell types. It binds to Vitamin D and its plasmametabolites and transport them to target tissues.

CASK PROTEIN Peripheral plasma membrane protein CASK is a protein thatin humans is encoded by the CASK gene. This protein is a multi domainscaffolding protein with a role in synaptic transmembrane proteinanchoring and ion channel trafficking. It interacts with thetranscription factor TBR1 and binds to several cell-surface proteinsincluding amyloid precursor protein, neurexins, and syndecans.

FIG. 8 relates to Q8 Gene Symbol=GC Vitamin D binding proteinPrecursor—Cask isoform 3 of Peripheral plasma membrane potein CASk—VIMVimentin

FIG. 9 relates to Q13 Gene Symbol=CASK Isoform 3 of Peripheral plasmamembrane protein CASK—HP HP protein

FIG. 10 relates to Q15 Gene Symbol—CASK Isoform 3 of Peripheral plasmamembrane protein CASK—IFNA13; IFNA1 Interferon alpha-1/13

AFCC is Prothombin Complex Concentrate (ProthoRAAS®) a combination ofblood clotting factors II, VII, IX and X or Factor IX.

Factor IX is one of several factors made in the liver with similarstructural properties.

Together with factors II (Prothombin), VII (proconvertin) and X(Stuart-Prower factor), factor IX (antihaemophilic factor B) comprisesthe so called prothombin complex group of factors, also known as PPSBfactors.

Owing to their similarity, the proteins in this group are usuallyisolated together in fraction III in the Cohn alcohol fractionationprocess.

They are then purified to give preparations containing all four factors,Prothombin complex concentrates (PCC).

ProthoRAAS are indicated currently for:

-   -   Haemophilia B—Prophylaxis, Bleeding, Surgery    -   Haemophilia A—Inhibitor treatment

Liver disease—Acute and chronic—active hepatitis, cirrhosis

Vitamin K deficiency—Oral anticoagulants, Obstructive jaundice,Malabsorption, changes in intestinal flora (antibiotics, Morbus Crohn,ulcerative colitis)

DIC (Disseminated Intravascular Coagulation)—Infection, Liver disease,obstetrical emergencies, surgical complications.

-   -   16. AFCC RAAS1 (Trade mark) (ProthoRAAS®+ApoA1+AT-III) for the        current indications as above together with all potential        indications as described.    -   17. AFCC RAAS 2 (Trade mark) (Prothombin Complex Concentrate        (ProthoRAAS®)+ApoA1+Human Albumin (AlbuRAAS®)), for the current        indications as above together with all potential indications as        described.    -   18. AFCC RAAS 3 (Trade mark) (Prothombin Complex Concentrate        (ProthoRAAS®)+ApoA1+Intravenous Immuno Globulin (GammaRAAS®)),        for the current indications as above together with all potential        indications as described.    -   19. AFCC RAAS 4 (Trade mark) (Prothombin Complex Concentrate        (ProthoRAAS®)+ApoA1+Intravenous Immuno Globulin (GammaRAAS®),        +Human Albumin (AlbuRAAS®)), for the current indications as        above together with all potential indications as described.    -   20. AFCC RAAS 5 (Trade mark) (Prothombin Complex Concentrate        (ProthoRAAS®)+ApoA1+Intravenous Immuno Globulin (GammaRAAS®),        +Human Albumin (AlbuRAAS®) and Fibrinogen (FibroRAAS®)), for the        current indications as above together with all potential        indications as described.    -   21. AFCC RAAS 6 (Trade mark) (Prothombin Complex Concentrate        (ProthoRAAS®)+ApoA1+Fibrinogen (FibroRAAS®)), for the current        indications as above together with all potential indications as        described.

2D Electropherosis of PCC:

Results of 2D eletropherosis of PCC not only the above four factorsproteins but also show a lot more proteins (Dots) that are beingidentified, as can be seen in FIG. 11.

2D Electropherosis of Fr. III:

2D electropherosis of Fraction III like Fraction IV contains a lot moreof proteins other than Thrombin, Prothombin Complex, as can be seen inFIG. 12. All these proteins are also being identified.

2D Electropherosis of Cryopaste:

2 D Electropherosis of Cryopaste results also show some other proteinswhich are being indentified Beside Fibrinogen and Factor VIII, as can beseen in FIG. 13.

In Vitro/Vivo Studies

-   -   1^(st) Production of 10 Batches totaling 200 grams for use in        VIVO study of Rabbits at Fudan University, Shanghai, China.

The 1^(st) 200 g AFOD was purified in East China University of Scienceand Technology using Process Nr 1, a flow chart for which is presentedin FIG. 14. The pilot production capability of that lab is about 5 kgper time. The purification process was modified according to theirequipments on site but the flow was same as we have done in thisDecember. The major differences are as following

-   -   1) The input of production was 5 kg of Fraction IV paste and        yield was about 25 g AFOD each time. Dr Li Chun Zhou produced 10        lots there to get 200 g AFOD;    -   2) The column used for AFOD purification was about 5 L DEAE        chromatography;    -   3) The centrifugation for collecting AFOD enriched pellet was        swing basket rotor centrifuge    -   4) Standing precipitation was used to get rid of celite;    -   5) For filling, manual filling was adopted;    -   6) No virus inactivation was used in the whole process.

The resulted AFOD was about 200 g for total 10 lots and all of AFOD werelyophilized.

The stabilizer used was mannitol and this product has been used toperform clinical studies on 52 rabbits in summer of 2008.

2^(nd) Pilot Production of 3 Lots at Shanghai RAAS Blood Products Co Ltd

2000 vials of AFOD RAAS (about 200 g) have been used in the following INVITRO studies:

-   -   1. Studies of 5 cancer cells line at RuiJin Hospital Shanghai        China.    -   2. Studies of 3 cancer cells line at R/D Lab Shanghai RAAS.    -   3. Studies of Bacteria at Microbiology Lab, Shanghai RAAS    -   4. Studies of Viruses HIV1,2 at NAT Lab, Shanghai RAAS

In the most recent pilot production, which was conducted in lastDecember at our Plant, we totally conducted 3 lots of production. It was25 kg Fraction IV for the 1^(st) lot, 50 kg for the rest of 2 lots. Thetotal yield was about 2000 vials of AFOD (about 200 g). There were about440 bottles of lyophilized, 660 vials of liquid with human albumin forstabilizer and another 880 bottles of liquid with mannitol forstabilizer.

-   -   1) We use continuous tube centrifugation to collect the AFOD        enriched pellet;    -   2) Using Filtration to get rid of celite;    -   3) A 15 L DEAD chromatography for AFOD purification;    -   4) Virus inactivation including SD and DV 20;    -   5) Automatic filling.

AFCC RAAS 1: A current product of Shanghai RAAS Blood products Co Ltdapproved for Sales in China and has been exported to a certain countryaround the globe. Product has been manufactured at large industrialscale.

Product has been used in the VITRO studies at Shanghai RAAS BloodProducts Co Ltd

-   -   1. 3 Cancer Cell lines at R/D Lab    -   2. Bacteria at Microbiology Lab    -   3. HIV 1+2 Testing at NAT Lab

In Vitro Studies of Cancer Cell Lines:

Procedures to test Cancer cells at RuiJin Hospital in Shanghai, China.

Cell Proliferation Assay by Using CCK 8 Test Kit Check all Reagents atLeast 3 Days Before Assay Reagents:

-   1. Cancer cell line: Human colon cancer cell line (HCT-116), Human    Breast cancer cell line (MCF-7), Human liver cancer cell line    (HepG2), Human pancreatic cancer cell line (PAC-1)-   2. CCK 8 (cell counting kit-8): Dojindo molecular technologies, Inc    (Maryland, US), product code # CK04-11-   3. Cell culture medium:    -   DMEM—high glucose 4.5 gm/L Gibco (invitorgen) 11965084    -   ANTIBIOTIC ANTIMYCOTIC Invitrogen 15240062    -   FBS Hyclone SH30071.03        4. AFOD: lyophilized formulation

Procedures: Day −3 Before Treatment

-   -   1. Pre-Warm up cell culture medium to 37 C (DMEM/10%        FBS/antibiotics)    -   2. Seed cells to a 15-cm dish and let cells grow 2-3 days to        reach 2*10⁸

Day −1 Before Treatment

-   -   1. Pre-Warm up cell culture medium to 37 C (DMEM/2%        FBS/antibiotics)    -   2. Seed cell at density of 2000/well in a 96-well plate.        Triplicate every treatment condition.        -   1) 0% AFOD        -   2) 2% AFOD        -   3) 10% AFOD    -   3. Leave cells for overnight growth

Day 0 of Treatment

-   -   1. Pre-Warm up cell culture medium to 37 C (DMEM/2%        FBS/antibiotics)    -   2. Change fresh medium in each for cells as following    -   1) 0% AFOD: Cancer cell+fresh DMEM/2% FBS/antibiotics    -   2) 2% AFOD: Cancer cell+1-4 diluted 10% AFOD with fresh DMEM/2%        FBS/antibiotics    -   3) 10% AFOD: Cancer cell+lyophilized AFOD dissolved in fresh        DMEM/2% FBS/antibiotics    -   4) Negative control: lyophilized AFOD dissolved in fresh DMEM/2%        FBS/antibiotics only    -   3. Incubate cells for 2-3 days and observe cell growth everyday

Day 1-2 after Treatment

Observation the proliferation of cells under microscopy

Day 3 after Treatment

-   -   1. Discard cell culture medium    -   2. Take picture of cell    -   3. Conduct the CCK8 assay according to manufacturer's        instruction

The antibiotics added in cell culture medium is basically to prevent thepotential bacterial or fugal contamination during the culture. Theantibiotics they added contains penicillin, streptomycin, andamphotericin B. Basically it won't kill cell and it is a routine recipein animal cell culture. And they also include a control in which cellsare cultured with DMEM/FBS/antibiotics only.

Reference is made to FIGS. 15-28.

The AFOD Anti-Tumor In Vitro Test Result

Procedures of Testing of cancer cells LS 174T (Colon), AGS (Gastric),and 45 (Gastric cancer cells at Shanghai RAAS R/D Lab procedures forboth product AFODRAAS 1 and AFCCRAAS 1

The dose dependent cell killing effect of AFOD by CCK8 assay is shown inFIG. 29.

Pictures of the cancer cells are shown in FIGS. 30 and 31.

Method and materials Used at Shanghai RAAS Blood Products Co Ltd R/DDept.

Reagents:

1. Cancer cell line: Human colon cancer cell line (HCT-116), HumanBreast cancer cell line (MCF-7), Human liver cancer cell line (HepG2),Human pancreatic cancer cell line (PAC-1)2. CCK 8 (cell counting kit-8): Dojindo molecular technologies, Inc(Maryland, US), product code # CK04-113. Cell culture medium:

DMEM - high glucose 4.5 gm/L Gibco (invitorgen) 11965084 ANTIBIOTICANTIMYCOTIC Invitrogen 15240062 FBS Hyclone SH30071.034. AFOD: lyophilized formulation

Procedures: Day −3 Before Treatment

-   -   5. Pre-Warm up cell culture medium to 37 C (DMEM/10%        FBS/antibiotics)    -   6. Seed cells to a 15-cm dish and let cells grow 2-3 days to        reach 2*10⁸

Day −1 Before Treatment

-   -   4. Pre-Warm up cell culture medium to 37 C (DMEM/2%        FBS/antibiotics)    -   5. Seed cell at density of 2000/well in a 96-well plate.        Triplicate every treatment condition.        -   4) 0% AFOD        -   5) 2% AFOD        -   6) 10% AFOD    -   6. Leave cells for overnight growth

Day 0 of Treatment

-   -   4. Pre-Warm up cell culture medium to 37 C (DMEM/2%        FBS/antibiotics)    -   5. Change fresh medium in each for cells as following    -   7. 0% AFOD: Cancer cell+fresh DMEM/2% FBS/antibiotics    -   8. 2% AFOD: Cancer cell+1-4 diluted 10% AFOD with fresh        DMEM/2%/FBS/antibiotics    -   9. 10% AFOD: Cancer cell+lyophilized AFOD dissolved in fresh        DMEM/2%/FBS/antibiotics    -   10. Negative control: lyophilized AFOD dissolved in fresh        DMEM/2% FBS/antibiotics only    -   6. Incubate cells for 2-3 days and observe cell growth everyday

Day 1-2 after Treatment

Observation the proliferation of cells under microscopy

Day 3 after Treatment

-   -   11. Discard cell culture medium    -   12. Take picture of cell    -   13. Conduct the CCK8 assay according to manufacturer's        instruction

FURTHER INVITRO STUDIES of MORE CANCERS CELL LINES are shown in FIGS.32-61.

INVITRO STUDIES of BACTERIA Performed at Shanghai RAAS Microbiology LabDue to the large dosage to kill bacteria while product available arelimited and saved for animal study of other diseases and cancers, Thisstudy does not completely kill all bacteria.

We performed bacteria experiments on AFOD RAAS 1 by both increasing thedosage of AFOD RAAS 1 and decreasing the density of testing bacteria.The current results will be listed in the following tables:

The amount of “+” in the following tables doesn't represent the accuratenumber of the testing bacteria remained in the medium after incubation;it represents the relative amount of them.

1. The Microbe Test with AFOD RAAS 1 on Staphylococcus aureus (a Kind ofAerobes)

16 AFOD added (ml) hours 24 hours 40 hours 72 hours 0.5 mlStaphylococcus None ++ ++++ ++++++++ aureus + 0 ml AFOD 0.5 mlStaphylococcus None ++ ++++ ++++ aureus + 8 ml AFOD 0.5 mlStaphylococcus None ++ ++++ ++++ aureus + 10 ml AFOD 0.5 mlStaphylococcus None None ++++ ++++ aureus + 12 ml AFOD

In this experiment, we increased the dosage of AFOD (8 ml; 10 ml; 12 ml)to the medium. We found that the liquid culture medium converted tosolid medium when we added 8 ml or more AFOD to the liquid medium andincubated for 24 hours. I think the main reason is the concentration ofAFOD we added was too high. So maybe it's a little difficult to increasethe dosage of AFOD anymore (such as 14 ml; 16 ml) even if the testingStaphylococcus aureus can still grow up when we added 12 ml AFOD to themedium.

2. The Microbe Test with AFOD RAAS 1 on Micrococcus luteus (a Kind ofAerobes)

AFOD added (ml) 16 hours 24 hours 40 hours 72 hours 0.5 ml MicrococcusNone None ++++ ++++++++ luteus + 0 ml AFOD 0.5 ml Micrococcus None None++ ++++++++ luteus + 8 ml AFOD 0.5 ml Micrococcus None None ++ ++++++++luteus + 10 ml AFOD 0.5 ml Micrococcus None None ++ ++++++++ luteus + 12ml AFOD3. The Microbe Test with AFOD RAAS 1 on Candida albicans (a Kind ofFungus)

AFOD added (ml) 48 hours 72 hours 96 hours 120 hours 0.5 ml Candida ++++++ ++++++++ ++++++++ albicans + 0 ml AFOD 0.5 ml Candida ++ ++++++++++++ ++++++++ albicans + 4 ml AFOD 0.5 ml Candida ++ ++++ ++++++++++++++++ albicans + 8 ml AFOD4. The Microbe Test with AFOD RAAS 1 on Aspergillus niger (a Kind ofFungus)

48 AFOD added (ml) hours 72 hours 96 hours 120 hours 0.5 ml Aspergillus++ ++++ ++++++++ ++++++++ niger + 0 ml AFOD 0.5 ml Aspergillus ++++++++++++ ++++++++ ++++++++ niger + 4 ml AFOD 0.5 ml Aspergillus ++++++++++++ ++++++++ ++++++++ niger + 8 ml AFOD

Reference is made to FIGS. 62-64.

HIV NAT Testing of AFODRAAS 1 and AFCC RAAS 1

Total HCV pos- pos- years samples positive % itive Percentage itivePercentage positive Percentage positive Percentage positive Percentage2006 633480 78 0.0123% 162 0.0256% 160 0.0253% 5 0.0008% 2 0.0003% 70.0011% 2007 345620 70 0.0203% 50 0.0145% 93 0.0269% 0 0.0000% 5 0.0014%6 0.0017% 2008 428422 23 0.0054% 43 0.0100% 108 0.0252% 0 0.0000% 10.0002% 18 0.0042% 2009 524299 17 0.0032% 45 0.0086% 110 0.0210% 00.0000% 3 0.0006% 0 0.0000% 2010 554297 53 0.0096% 31 0.0056% 1310.0236% 0 0.0000% 5 0.0009% 0 0.0000% 2006~2010 2486118 241 0.0097% 3310.0133% 602 0.0242% 5 0.0002% 16 0.0006% 31 0.0012%

The above table show HCV,HIV1,2 and HBsAg on the left are Elisa testingHCV-RNA HIVRNA, HBV DNA are results of NAT Testing at Shanghai RAAS NATLaboratory for A total of units of plasma 2,486,188 during five yearsperiod from 2006 to 2010. Out of These number of units, there were 241Tested positive HCV by Elisa, Confirmed HCV Positive by NAT is only 5units so a total of 236 units are FALSE POSITIVE by Elisa Method. From2007 to 2010 there is NO HCV POSITIVE from our donor Populationtherefore

We have No Hepatitis B Virus to test for our study. Further study willbe done when receiving samples from Infectious disease hospital inShanghai which will also carry out Animal study for all HIV, HCV andHBV.

For HIV 1,2 by Elisa had 331 Positive and Confirmed by NAT is only 16 soFalse Positive Is 315 Units. Luckily our R/D still had 1 sample ofPOSITIVE HIV1,2 to conduct this study. For HBV we had a total of 602Positive by Elisa and 31 confirmed by NAT Total False Positive by Elisais 571 Samples. In 2009 and 2010 we had no Positive Sample confirmed ByNAT.

To avoid the large dosage of limited AFODRAAS and AFCCRAAS, NAT Lab hasdiluted the positive plasma sample to weaken the presence of HVI1,2virus to the level of 1:3200 and the first test result is as below forthe HIV Positive Plasma to use as A CONTROL.

HIV positive plasma(60051215) 5.9 E+6 IU/mlthe plasma(1:100) 3 E+5 IU/mlthe plasma(1:200) 1.1 E+5 IU/mlthe plasma(1:400) 5.4 E+4 IU/mlthe plasma(1:800) 2.9 E+4 IU/mlthe plasma(1:1600) 1.4 E+4 IU/mlthe plasma(1:3200) 5.7 E+3 IU/mlSample incubation at room temperature until Day 3 Concentration20 ml of the plasma(1:800)+2 bottles of AFODRAAS1 2.3 E+4 IU/ml20 ml of the plasma(1:1600)+2 bottles of AFODRAAS 1 5.9 E+3 IU/ml20 ml of the plasma(1:3200)+2 bottles of AFODRAAS1 1.9 E+3 IU/ml20 ml of the plasma(1:800)+2 bottles of AFCCRAAS 1 1.3 E+4 IU/ml20 ml of the plasma(1:1600)+2 bottles of AFCC RAAS 1 2.9 E+3 IU/ml20 ml of the plasma(1:3200)+2 bottles of AFCC RAAS 1 56 IU/ml

As shown in the table above, we have observed HIV1,2 Positive Samplemixed With AFODRAAS 1 and AFCC RAAS 1 have reduced Number of IU/MI

The second test results show as below there is a significant drop from29000 IU/ml of Positive Plasma Control down to 4500 IU/ml due to thedecade of HIV1,2 Virus in the plasma; Thus we conduct further test toassure by using NON DILUTED SAMPLES even though we have to increasedosage of AFOD RAAS1 and AFCCRAAS 1 to cope with high concentration ofHIV1,2 virus. However it is an experimental test that needs furtherSTUDIES.

Initial Sample concentration Day 3 Concentration the positive 29000IU/ml 4500 IU/ml plasma(1:800) the positive 14000 IU/ml 2100 IU/mlplasma(1:1600) the positive  5700 IU/ml  670 IU/ml plasma(1:3200) 20 mlof the positive 29000 IU/ml 13000 IU/ml  plasma(1:800) + 2 bottles ofAFODRAAS 1 20 ml of the positive 14000 IU/ml 6300 IU/ml plasma(1:1600) +2 bottles of AFODRAAS 1 20 ml of the positive  5700 IU/ml 2500 IU/mlplasma(1:3200) + 2 bottles of AFODRAAS1 20 ml of the positive 29000IU/ml 4600 IU/ml plasma(1:800) + 2 bottles of AFCC RAAS1 20 ml of thepositive 14000 IU/ml  620 IU/ml plasma(1:1600) + 2 bottles of AFCC RAAS1 20 ml of the positive 5700 IU/ml  130 IU/ml plasma(1:3200) + 2 bottlesof AFCC RAAS1 20 ml of the positive 29000 IU/ml 22000 IU/ml plasma(1:800) + 1 bottle of AFODRAAS + 1 bottle of AFCC 20 ml of thepositive 14000 IU/ml 2800 IU/ml plasma(1:1600) + 1 bottle of AFODRAAS +1 bottle of AFCC 20 ml of the positive  5700 IU/ml  110 IU/mlplasma(1:3200) + 1 bottle of AFODRAAS + 1 bottle of AFCC

In Vivo Study Experimental Design and Results of Pilot ScalePre-Clinical Animal Test of AFOD RAAS 1—for the Antiatherogenic andCholesterol-Lowing Properties 1. Purpose of the Experiments: 1.1 to Testthe Effects of AFOD RAAS 1 for the Suppression of Fatty Streak Lesions.1.2. To Test the Efficiency of Making Animal Models for Atherosclerosis1.3 to Test the Efficacy and Dosage for AFOD RAAS 1 in the Suppressionof Fatty Streak Lesions and Cholesterol-Related Plasma Indicators 2.Experimental Design

2.1 Experimental Animals. Male New Zealand White-Ear or Other StrainHealthy Rabbits (2.0 Kg Body Weight, 4 in Each Group) were Used in theExperiment.

2.2 Experimental Model Construction

The rabbits were fed with normal diet under regular lab conditions for5-10 days. The rabbits were fasted for 12 hrs before the beginning ofthe experiments. Blood parameters were then tested as the normal levelof plasma indicators. The animals were then randomly grouped for theexperiment.

2.3 Treatments

After grouping of the experimental animals, they were switched tohigh-fat diet. Body weight and plasma parameters were tested andrecorded once every two weeks until indicators shown to have lipidmetabolism disorders and the formation of obvious fatty streak lesionsin blood vessels. The animals were switched from high-fat diet to normaldiet. These are the grouping of the experimental animals: (1) positivecontrol group, (2) AFOD RAAS 1-Al treatment group was further dividedinto high, medium and low three dose sub-groups. During the first 4weeks of the AFOD RAAS 1-treatment, plasma parameters and animal generalconditions were carefully monitors and recorded. At the end of theexperiments, the lab animals were sacrificed for pathological andanatomical analysis.

2.4 Parameters Tested: 1) Blood Cholesterol-Related Parameters:

-   -   TC: total cholesterol    -   TG: tri-gliceride    -   LDL-C: low density lipoprotein—LDL    -   VLDL-C: very low density lipoprotein—VLDL    -   HDL-C: high density lipoprotein—HDL    -   TC/HDL-C or (LDL-C+VLDL-C)/HDL-C: ratio

2) Pathological Tests

-   -   pathology in aorta (main artery)

3) Liver Index 3. Experimental Process

A total of 52 rabbits were purchased at different time, four of themwere used as normal control and fed with normal diet the whole timeduring the experiments. There rest of the animals was switched to highfat diet.

Some of the lab animals showed stomach symptoms after switched tohigh-fat diet and died within 4 weeks. From week 7 to week 10, 6 morelab animals died for the same reason. At week 10 and 11, two animalswere sacrificed as animal model control. These two animals weredissected to obtain aorta, heart and liver tissue samples. Observation:the appearance of the aorta and liver were observed and recorded. Theinside surface of aorta has obvious fatty streak deposit and lesion. Theliver tissue has white fatty tissue deposit. Taken together, theconstruction of the animal models was successful. Two lab animals fromthe normal control group were also sacrificed and dissected. Noabnormality of aorta and liver tissues were observed.

The rest 34 rabbits were then switched to normal diet and grouped intoanimal-model group, positive control group and low, medium and highdosage AFOD RAAS 1-Al treatment groups.

Animal-model group (no AFOD RAAS 1 and normal diet): 4Positive control: 5AFOD RAAS 1-Al treatment group:High dosage group (100 mg/each), average body weight 2.8 kg: 11Medium dosage group (50 mg/each): 8Low dosage group (25 mg/each): 6

After 4 weeks of treatment, two lab animals from the high-dosage groupwere sacrificed and dissected. No significant changes of fatty streaklesions were observed. Based on this observation, all of the lab animalsfrom the experimental groups were switched to high-dosage AFOD RAAS 1treatment, which is 100 mg/each.

4. Experimental Results 4.1 Duration of the Animal Model Construction

After feeding of the lab animals with high-fat diet (1.5% cholesterol,3% lard, and normal feed) for four weeks, all cholesterol-related plasmaparameters were increased significantly (see attached data sheet). Atweek 4, one of the lab animals were sacrificed and showed limited amountof fatty streak lesions. At week 10 and week 11, five lab animals weresacrifices and dissected. Obvious fatty streak lesions can be observedon the inside surface of the aorta. Fat deposit can also be observed onthe liver tissues.

Conclusion: At week 10-11, fatty streak lesions were formed.

4.2 Successful Rate for Model Construction

During the animal model construction, 7 animals died during the first 4weeks of high-fat diet due to stomach symptoms. Between week 7-10, 6more lab animals died because of high-fat. The mortality rate is 16.7%.These lab animals were also dissected and 90% of them the aorta tissueshowed fatty streak lesions occupied 20% of the total area.

Conclusion: the successful rate of model construction is 60%.

Models (high fat diet, execute at 10 weeks, the picture of the aorta,with a Plaque area=24.3%) is shown in FIG. 65. Reference is also made toFIG. 66.

Control group (build up the animal models, without AFOD RAAS 1, thennormal diet for 4 weeks) Plaque area=45.3%, as can be appreciated fromFIG. 67.

Control groups (build up the animal models, without AFOD RAAS 1, thennormal diet for 8 weeks). FIG. 68 shows a Plaque area=98.5%, and FIG. 69shows a plaque area=78.94%.

4.3 Plasma Parameters

1) First 8 weeks of treatment (n=7, for the first 4 weeks, AFOD RAAS 1was administered once a week and 100 mg/each; in the following 4 weeks,50 mg/each were administered twice a week)

TC/ HDL- Weight TG TCH VLDL-C HDL-C LDL-C C Start 2.164 0.967 1.1520.870 0.748 0.282 1.938 Before 2.7 5.191 36.153 14.996 8.261 21.1576.560 After 2.79 1.17 3.69 1.09 1.46 2.60 3.0002) At week 11 of the experiment (n=7, for the first 4 weeks, AFOD RAAS 1was administered once a week and 100 mg/each; in the following 4 weeks,50 mg/each were administered twice a week, for the last 3 weeks, 100mg/each were administered once a week)

TC/ HDL- Weight TG TCH VLDL-C HDL-C LDL-C C Start 2.2 0.93 1.430 0.9580.432 0.472 4.185 Before 2.45 4.507 34.683 15.443 10.168 19.24 3.667After 2.65 1.94 3.322 1.14 1.17 2.19 3.8443) Positive control (crestol, administered 4 weeks)

TC/ HDL- Weight TG TCH VLDL-C HDL-C LDL-C C Start 2.25 0.450 0.946 0.5090.539 0.437 1.844 Before 2.85 9.122 20.339 9.710 8.404 10.911 4.511After 3.1 0.474 8.535 3.675 1.25 4.86 6.8114) control (statin) (n=4)

TC/ HDL- Weight TG TCH VLDL-C HDL-C LDL-C C Start 2.113 0.843 1.4440.885 0.684 0.559 2.108 Before 2.742 2.666 32.42 7.467 5.657 24.9539.459 End 3.1 1.207 5.277 1.961 0.759 3.316 6.4585) Summary of plasma parameter data

Model Group Week 8 TC/ VLDL- HDL- Weight TG TCH C HDL-C LDL-C C −0.050−0.343 −31.114 −9.225 −8.484 −21.889 2.003 −0.020 −1.995 −21.839 −4.053−5.763 −17.786 0.345 −0.020 −1.632 −26.320 −0.570 −4.698 −25.750 2.9180.250 −1.866 −29.300 −8.175 −4.648 −21.125 0.303 Sum 0.160 −5.836−108.573 −22.023 −23.593 −86.550 5.568 Ave 0.023 −0.834 −15.510 −3.146−3.370 −12.364 0.795

AFOD RAAS 1 Group Week 8 Weight TG TCH VLDL-C HDL-C LDL-C TC/HDL-C 0.200−19.259 −28.873 −5.730 −17.483 −23.143 1.863 0.250 −4.061 −25.631−12.718 −9.323 −12.913 −0.034 0.200 −0.487 −26.677 −14.607 −5.932−12.070 −2.164 −0.100 0.677 −31.438 −13.629 −4.971 −17.809 −2.739 −0.100−0.211 −39.804 −15.867 −3.983 −23.937 −6.655 0.200 −3.394 −41.059−23.550 −1.933 −17.509 −13.858 0.000 −1.432 −33.792 −11.265 −3.955−22.527 −4.051 Sum 0.650 −28.167 −227.274 −97.366 −47.580 −129.908−27.638 Ave 0.093 −4.024 −32.468 −13.909 −6.797 −18.558 −3.948 ApoAI0.0500 ± 0.1658 −1.1028 ± 1.8167 −31.4684 ± 5.7427 −13.6172 ± 1.7595−5.6328 ± 2.2182 −17.8512 ± 5.4016 −3.1286 ± 2.4466 (n = 5) Model 0.0400± 0.1407 −1.4590 ± 0.7590 −27.1432 ± 4.0510  −5.5058 ± 3.9762 −5.8982 ±1.7989 −21.6375 ± 3.2697  1.3920 ± 1.2890 group P value 0.926 0.7270.246 0.004 0.852 0.26 0.013

Conclusion: After 8 weeks of AFOD RAAS 1 treatment, allcholesterol-related plasma parameters decreased. There is also adecrease in the model control group. Significant changes can only beobserved in VLDL-C and TC/HDL-C (p<0.05). There is no significant changefor the rest of the parameters.

AFOD RAAS 1 group Week 11 Weight TG TCH VLDL-C HDL-C LDL-C TC/HDL-C0.200 −4.241 −30.064 −8.388 −10.183 −21.676 1.294 0.300 −3.740 −31.052−7.169 −8.799 −23.883 −2.282 0.000 0.092 −29.618 −19.679 −11.844 −9.939−0.164 0.300 −2.374 −34.708 −21.989 −5.151 −12.719 −1.978 Sum 0.800−10.263 −125.442 −57.225 −35.977 −68.217 −3.129 Ave 0.200 −2.566 −31.361−14.306 −8.994 −17.054 −0.782

Weight TG TCH VLDL-C HDL-C LDL-C TC/HDL-C Model 0.0400 ± 0.1407 −1.4590± 0.7590 −27.1432 ± 4.0510 −5.5058 ± 3.9762 −5.8982 ± 1.7989 −21.6375 ±3.2697  1.3920 ± 1.2890 AFOD 0.2000 ± 0.1414 −2.5658 ± 1.9396 −31.3605 ±2.3107 −14.3062 ± 7.6126 −8.9942 ± 2.8486 −17.0542 ± 6.7679 −0.7824 ±1.6706 RAAS 1 11 wk P value 0.689 0.99 0.532 0.11 0.658 0.583 0.795

Conclusion: All cholesterol-related parameters showed significantdecrease. But compared with the control group, there is no statisticalsignificance.

6) Changes of HDL-C:

AFOD RAAS 1 Fold normal treatment increase increase  8 wks 0.748 1.4640.716 1.436 11 wks 0.432 1.423 0.992 3.078 control 0.684 0.759 0.0740.102

Compare the HDL-C values before and after the treatment, it indicatedthat HDL-C is elevated after AFOD RAAS 1-Al treatment

Conclusion, iv infusion of AFOD RAAS 1 could lower blood cholesterolthrough the formation of HDL.

The invention reveals that all healthy good cells have eaten all fats(BAD CELLS and damaged cells as described in the function of the livernot through the formation of HDL. In this preliminary and small study,The Inventor has found that even with the longer And higher dosage ofAFOD RAAS 1Group 2, the formation of HDL has been reduced to 54.15% from92.36% of AFODRAAS 1 Group 1 and the Total of TC/HDL-C is −53.55% muchhigher than to compare with AFODRAAS 1 Group 2 which has TC/HDL-C−40.48%

To prove it, Atorvastatin® was also used in this study when comparingwith control group, it has significantly reduced TG −60.73% andincreased HDL to 64.69% however TCH have increased to 61.74%, VLDL-Cincreased 87.40% LDL-C increased 46.56% and TC/HDL-C is 5.47%. Inconclusion it can reduces TG and increases HDL but will NOT LOWER BadCholesterol VLDL-C, LDL-C, TCH and TC/DHL-C

Drugs like Atorvastatin @cannot remove FATS from PLAQUE whereasAFODRAAS1 and AFCCRAAS1 CAN REMOVE FATS from PLAQUE, CLEAN the arteries.

In the first year of high school, we began to learn that when the YELLOWCOLOR Mixed with BLUE, it turns GREEN. In a drug if you have to have aYELLOW COLOR and BLUE COLOR for your final product, It is IMPOSSIBLE asthe final product will turn GREEN. This is the reason why ChemicalsREACT that is why most of drugs from Chemicals have SIDE EFFECTS.

There is only ONE MANUFACTURER, MODERATOR, REGULATOR and DISTRIBUTORwhich can produce the product which maintains the YELLOW COLOR and BLUECOLOR is THE LIVER producing PILE approximately 0.5-0.9 liter of PILEper day. PILE is a LIQUID which has YELLOW COLOR and BLUE COLOR.

Reference is made to FIGS. 70-76.

Therefore in this case, ATORVASTATIN® is one among thousands of drugsavailable can be combined with AFODRAAS1-85 or AFCC RAAS1-85 to enhancethe EFFICACY of the drugs. Before this invention, Drugs likeATORVASTATIN® and LIPITOR® have helped a lot of people with HIGHCHOLESTEROL.

Weight TG TCH VLDL-C HDL-C LDL-C TC/HDL-C control 3.1 1.207 5.277 1.9610.759 3.316 6.458 AFOD 1 2.79 1.17 3.69 1.09 1.46 2.6 3 compare tocontrol −10.00% −3.07% −30.07% −44.42% 92.36% −21.59% −53.55% AFOD 22.65 1.94 3.322 1.14 1.17 2.19 3.844 compare to control −14.52% 60.73%−37.05% −41.87% 54.15% −33.96% −40.48% Atorvastatin 3.1 0.474 8.5353.675 1.25 4.86 6.811 compare to control 0.00% −60.73% 61.74% 87.40%64.69% 46.56% 5.47%

Liver

1) Liver surface: When the animal models were first made, the liversurface of the lab animals from the animal-model group showed abnormalwhite colored spots. Histological analysis showed that it is???. Thesurface of the liver feels harder than normal tissue. The liver samplestaken from the −Al treated group has fewer???. The surface is not astough as when the animal model was first made. The un-treated group alsoshowed relief in the??? and softened. The probable reason is thatbecause the high cholesterol and atherosclerosis model is made in ashort period of time, the switch to normal diet also helped to reliefthe symptoms.2) Liver index

weight Liver (g) index ApoAI 8 weeks 0.09 0.033 ApoAI 11 weeks 0.1170.044 model control 0.111 0.036

The liver index did not show any changes after the AFOD RAAS 1treatment.

6 Fatty Streak Lesions

Compare Compare to Increase to model Decrease Area control % control %AFOD RAAS 1 43.84 19.03 77 −27.36 38.43 8 wk AFOD RAAS 1 50.51 25.71 104−20.69 29.05 11 wk Model control 71.20 46.39 187 Model first 24.81 made1) Fatty streak lesion appearance: the tissue from the non-AFOD RAAS1-group (model control) has bumps on the surface. The tissue feelstender and hard as touched with bare hand. Dissection of the bloodvessels showed fat deposit in the cross-section of the tissue. The fattystreak lesion decreases as the aorta descends. Compare with the modelcontrol group, the AFOD RAAS 1-group do not have bumps in the bloodvessel surface. The tissue feels soft as touched with bare hand.2) Area measurement of the fatty streak lesion: Compare with themodel-control group, the surface area of the fatty streak lesionincreased 77% and 104%, and the non-AFOD RAAS 1-treated group increasedby 187%. Compare with the non-AFOD RAAS 1-Al treated group, the fattystreak lesion of the AFOD RAAS 1-group decreased by 38.43% at week 8 anddecreased by 29.05% at week 11.

Conclusion: Administration of AFOD RAAS 1 to the lab animals withatherosclerosis obviously suppresses the further development of fattystreak lesion.

Drugs like Atorvastatin @cannot remove FATS from PLAQUE whereasAFODRAAS1-85 and AFCCRAAS1-85 CAN REMOVE FATS from PLAQUE, CLEAN thearteries.

FIG. 77 shows Normal (normal diet 8 weeks) and FIG. 78 shows Plaquearea=0.

FIGS. 79 and 80 show build up the animal models, with AFOD RAAS 1-A1 8weeks.

FIG. 79 shows Plaque area=13.29%, and FIG. 80 shows Plaque area=20.5%.

FIGS. 81 and 82 show build up the animal models, with AFOD RAAS 1 8weeks (another rabbit). FIG. 81 shows Plaque area=58.4%, and FIG. 82shows Plaque area=82.17%.

FIGS. 83-85 show Group with AFOD RAAS 1 11 weeks. FIG. 83 shows Plaquearea=47.27%, FIG. 84 shows Plaque area=40.32%, and FIG. 85 shows Plaquearea=51.13%.

3) Analysis of lipid content at dissected aorta

lipid con. (umol/mg) sig  8 weeks (n = 7)  0.025 ± 0.0095 0.006 p < 0.0111 weeks (n = 4 0.0267 ± 0.0054 0.015 p < 0.05 positive control (n = 4)0.0274 ± 0.006  0.046 p < 0.05 Control (n = 4) 0.0736 ± 0.014 

Conclusion: Comparing with the model control group, the triglyceridecontent at dissected aorta of the AFOD RAAS 1 treated group issignificantly lowered. The decrease is significant statistically.(p<0.05).

5. Experimental Summary

The purpose of this pilot-scale preclinical animal test of AFOD RAAS 1is the successful rate and time estimate of making animal model ofatherosclerosis, dose and effects human AFOD RAAS 1-Al administration onthe blood cholesterol-related levels and the suppression of developmentof fatty streak lesion.

Based on data collected from the experiment, successful making of a highcholesterol rabbit model need 4-5 weeks. The formation ofatherosclerosis fatty streak lesion need more than 10 weeks of high-fatdiet (at week 10-11, the average surface area of fatty streak lesion is24%). The successful rate for model making is 60%. After intravenousinfusion of human AFOD RAAS 1 at 100 mg/wk for 8-11 weeks, thehypercholesterolemia and liver lesion improved dramatically, but thedoes not stop the formation of fatty streak lesion at aorta. Thus, thehypercholesterolemia and liver lesion can slowly regress after switch tolow fat diet, but the atherosclerosis fatty streak lesion progresses andneed to be treated.

The experiment shows that the administration of AFOD RAAS 1 tohypercholesterolemia lab animals reduces the surface area of fattystreak lesion at aorta and decreases the triglyceride content in thelesion tissue, thus; AFOD RAAS 1 has the potential to be developed to bea antiatherogenic and cholesterol-lowing medicine.

TABLE 1 The change of plasma lipid parameter 1. Wk0, wk10 and wk18 meanthe actual value of each parameter. 2. Wk18-wk0 (or wk21-wk0) means thechange calculated by comparing the value of wk 18 (or wk21) to the valueof wk 0. This means the overall results during the whole process, whichmeans (high fat diet + switch to normal diet + different treatment). Itis calculated by % of change = (value of wk18 − value of wk 0)/value ofwk 0. 3. Wk18-wk10 (or wk21-wk10) means the change calculated bycomparing the value of wk 18 (or wk21) to the value of wk 10. Thisrepresents the results during the second half process, which means(switch to normal diet + different treatment). It is calculated by % ofchange = (value of wk18 − value of wk 10)/value of wk 10.4. Please refer to table 2 for the experiment design

AFODRAAS 1 treatment for 8 weeks Weight TG TCH VLDL-C HDL-C LDL-CTC/HDL-C wk0 2.164 0.967 1.152 0.87 0.748 0.282 1.938 wk10 2.7 5.19136.153 14.996 8.261 21.157 6.56 wk18 2.79 1.17 3.69 1.09 1.46 2.6 3wk18-wk0 28.93% 20.99% 220.31% 25.29% 95.19% 821.99% 54.80% wk18-wk103.33% −77.46% −89.79% −92.73% −82.33% −87.71% −54.27%

AFODRAAS 1 treatment for 11 weeks Weight TG TCH VLDL-C HDL-C LDL-CTC/HDL-C Wk 0 2.2 0.93 1.43 0.958 0.432 0.472 4.185 Wk 10 2.45 4.50734.683 15.443 10.168 19.24 3.667 Wk 21 2.65 1.94 3.322 1.14 1.17 2.193.844 wk21-wk0 20.45% 108.60% 132.31% 19.00% 170.83% 363.98% −8.15%wk21-wk10 8.16% −56.96% −90.42% −92.62% −88.49% −88.62% 4.83%

Atorvastatin Atorvastatin for 4 weeks Weight TG TCH VLDL-C HDL-C LDL-CTC/HDL-C Wk 0 2.25 0.45 0.946 0.509 0.539 0.437 1.844 Wk 10 2.85 9.12220.339 9.71 8.404 10.911 4.511 Wk 18 3.1 0.474 8.535 3.675 1.25 4.866.811 wk18-wk0 37.78% 5.33% 802.22% 622.00% 131.91% 1012.13% 269.36%wk18-wk10 8.77% −94.80% −58.04% −62.15% −85.13% −55.46% 50.99%

control Weight TG TCH VLDL-C HDL-C LDL-C TC/HDL-C Wk 0 2.113 0.843 1.4440.885 0.684 0.559 2.108 Wk 10 2.742 2.666 32.42 7.467 5.657 24.953 9.459Wk 18 3.1 1.207 5.277 1.961 0.759 3.316 6.458 wk18-wk0 46.71% 43.18%265.44% 121.58% 10.96% 493.20% 206.36% wk18-wk10 13.06% −54.73% −83.72%−73.74% −86.58% −86.71% −31.73%

TABLE 2 The experiment design

TABLE 3 change of fatty streak lesions Fatty Compare to Compare tostreak wk 10 of wk 18 of Time lesions control control point area (%)group Increase % group Decrease % AFODRAAS 1 Wk 18 43.84 19.03 77 −27.3638.43 Group 1 AFODRAAS 1 Wk 21 50.51 25.71 104 −20.69 29.05 Group 2Atrovastatin Wk 18 71.20 46.39 187 Control group Wk 10 24.81

TABLE 4 Analysis of lipid content at dissected aorta P value (comparedto Lipid con. (umol/mg) control group) AFODRAAS 1 Group 1  0.025 ±0.0095 0.006 (n = 7) AFODRAAS 1 Group 2  0.0267 ± 0.0054 0.015 (n = 4)Atorvastatin group (n = 4) 0.0274 ± 0.006 0.046 Control group (n = 4)0.0736 ± 0.014 Weight TG TCH VLDL-C HDL-C LDL-C TC/HDL-C control 3.11.207 5.277 1.961 0.759 3.316 6.458 AFOD 1 2.79 1.17 3.69 1.09 1.46 2.63 compare to −10.00% −3.07% −30.07% −44.42% 92.36% −21.59% −53.55%control AFOD 2 2.65 1.94 3.322 1.14 1.17 2.19 3.844 compare to −14.52%60.73% −37.05% −41.87% 54.15% −33.96% −40.48% control Atorvastatin 3.10.474 8.535 3.675 1.25 4.86 6.811 compare to 0.00% −60.73% 61.74% 87.40%64.69% 46.56% 5.47% control

Results of Studies in Comparison with Control

1. A method of introducing healthy good human cells to eat up baddamaged cells, comprising administering an effective amount of a healthygood protein containing transferrin, alpha 1-antitrypsin, apolipoproteinA and human albumin.
 2. The method of claim 1, further comprisingadministering an effective amount of a healthy good protein containingApoA1/2/4.
 3. The method of claim 1, wherein the protein containstransferrin.
 4. The method of claim 1, wherein the protein containsalpha 1-antitrypsin.
 5. The method of claim 1, wherein the proteincontains a C1 esterase inhibitor.
 6. The method of claim 1, furthercomprising administering an effective amount of a healthy good proteincontaining Factor II, Factor VII, Factor IX and Factor X in prothrombincomplex concentrate.
 7. The method of claim 1, wherein the proteincontains human albumin.
 8. The method of claim 1, further comprisingadministering an effective amount of a good healthy protein containingimmunoglobulin.
 9. A method of reducing damage to healthy human cells,comprising administering an effective amount of a healthy good proteincontaining fibrinogen.
 10. The method of claim 9, further comprisingadministering an effective amount of a healthy good protein containingFactor VIII.
 11. The method of claim 9, further comprising administeringan effective amount of a healthy good protein containing highconcentrate fibrinogen.
 12. The method of claim 9, further comprisingadministering an effective amount of a healthy good protein containingthrombin.
 13. The method of claim 9, further comprising administering aneffective amount of a healthy good protein containing hepatitis B immuneglobulin (HBIG).
 14. The method of claim 9, further comprisingadministering an effective amount of a healthy good protein containinganti-thrombin III (AT-III).
 15. The method of claim 9, furthercomprising administering an effective amount of a healthy good proteincontaining protein C.
 16. The method of claim 9, further comprisingadministering an effective amount of a healthy good protein containingfibronectin.
 17. The method of claim 9, further comprising administeringan effective amount of healthy good protein S.
 18. The method of claim9, further comprising administering an effective amount of healthy goodprotein M.
 19. The method of claim 9, further comprising administeringan effective amount of all healthy good proteins in Fraction III ofplasma where the concentration of healthy good cells is a macrophage.20. The method of claim 9, further comprising administering an effectiveamount of a protein including a healthy good cell macrophage in whiteblood cells, red blood cells, platelets, chylomicrons, electrolyses,peptides in human or in animal or chemicals or substances from anysource of materials to obtain the cells for further purification. 21.The method of claim 9, further comprising administering an effectiveamount of a protein including a healthy good cell neutrophil in whiteblood cells, red blood cells, platelets, chylomicrons, electrolyses,peptides in human or in animal or chemicals or substances from anysource of materials to obtain the cells for further purification. 22.The method of claim 9, further comprising administering an effectiveamount of a protein including a healthy good cell basophil in whiteblood cells, red blood cells, platelets, chylomicrons, electrolyses,peptides in human or in animal or chemicals or substances from anysource of materials to obtain the cells for further purification. 23.The method of claim 9, further comprising administering an effectiveamount of a protein including a healthy good cell lymphocyte in whiteblood cells, red blood cells, platelets, chylomicrons, electrolyses,peptides in human or in animal or chemicals or substances from anysource of materials to obtain the cells for further purification. 24.The method of claim 9, further comprising administering an effectiveamount of a protein including a healthy good cell eosinophil in whiteblood cells, red blood cells, platelets, chylomicrons, electrolyses,peptides in human or in animal or chemicals or substances from anysource of materials to obtain the cells for further purification.
 26. Amethod of introduction of a healthy good human cells to eat up baddamaged cells, comprising administering an effective amount of a proteincontaining at least one of the following apolipoproteins: ApoA1, ApoA2,ApoA4, Apo-B48, ApoB100, ApoCI, ApoCII, ApoCIII, Apo-D, Apo-E, Apo-H,and Apo(a), all of which contain good healthy cells.
 27. The method ofclaim 26, wherein the protein further contains at least one of thefollowing: alpha 1 antitrypsin (A1AT), transferrin, and human albumin,all of which contain good healthy cells.